Journal of Structural Biology: X最新文献_第8页

Measurement of local resolution in electron tomography 电子断层扫描局部分辨率的测量

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2019.100016

J.L. Vilas , J. Oton , C. Messaoudi , R. Melero , P. Conesa , E. Ramirez-Aportela , J. Mota , M. Martinez , A. Jimenez , R. Marabini , J.M. Carazo , J. Vargas , C.O.S. Sorzano

{"title":"Measurement of local resolution in electron tomography","authors":"J.L. Vilas , J. Oton , C. Messaoudi , R. Melero , P. Conesa , E. Ramirez-Aportela , J. Mota , M. Martinez , A. Jimenez , R. Marabini , J.M. Carazo , J. Vargas , C.O.S. Sorzano","doi":"10.1016/j.yjsbx.2019.100016","DOIUrl":"10.1016/j.yjsbx.2019.100016","url":null,"abstract":"<div><p>Resolution (global and local) is one of the most reported metrics of quality measurement in Single Particle Analysis (SPA). However, in electron tomography, the situation is different and its computation is not straightforward. Typically, resolution estimation is global and, therefore, reduces the assessment of a whole tomogram to a single number. However, it is known that tomogram quality is spatially variant. Still, up to our knowledge, a method to estimate local quality metrics in tomography is lacking. This work introduces <em>MonoTomo</em>, a method developed to estimate locally in a tomogram the highest reliable frequency component, expressed as a form of local resolution. The fundamentals lie in a local analysis of the density map via monogenic signals, which, in analogy to <em>MonoRes</em>, allows for local estimations. Results with experimental data show that the local resolution range that MonoTomo casts agrees with reported resolution values for experimental data sets, with the advantage of providing a local estimation. A range of applications of <em>MonoTomo</em> are suggested for further exploration.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2019.100016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137262","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 11

Small angle X-ray scattering and molecular dynamic simulations provide molecular insight for stability of recombinant human transferrin 小角度x射线散射和分子动力学模拟为重组人转铁蛋白的稳定性提供了分子视角

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2019.100017

Alina Kulakova , Sowmya Indrakumar , Pernille Sønderby , Lorenzo Gentiluomo , Werner Streicher , Dierk Roessner , Wolfgang Frieß , Günther H.J. Peters , Pernille Harris

{"title":"Small angle X-ray scattering and molecular dynamic simulations provide molecular insight for stability of recombinant human transferrin","authors":"Alina Kulakova , Sowmya Indrakumar , Pernille Sønderby , Lorenzo Gentiluomo , Werner Streicher , Dierk Roessner , Wolfgang Frieß , Günther H.J. Peters , Pernille Harris","doi":"10.1016/j.yjsbx.2019.100017","DOIUrl":"10.1016/j.yjsbx.2019.100017","url":null,"abstract":"<div><p>Transferrin is an attractive candidate for drug delivery due to its ability to cross the blood brain barrier. However, in order to be able to use it for therapeutic purposes, it is important to investigate how its stability depends on different formulation conditions. Combining high-throughput thermal and chemical denaturation studies with small angle X-ray scattering (SAXS) and molecular dynamics (MD) simulations, it was possible to connect the stability of transferrin with its conformational changes. Lowering pH induces opening of the transferrin N-lobe, which results in a negative effect on the stability. Presence of NaCl or arginine at low pH enhances the opening and has a negative impact on the overall protein stability.</p></div><div><h3>Statement of Significance</h3><p>Protein-based therapeutics have become an essential part of medical treatment. They are highly specific, have high affinity and fewer off-target effects. However, stabilization of proteins is critical, time-consuming, and expensive, and it is not yet possible to predict the behavior of proteins under different conditions. The current work is focused on a molecular understanding of the stability of human serum transferrin; a protein which is abundant in blood serum, may pass the blood brain barrier and therefore with high potential in drug delivery. Combination of high throughput unfolding techniques and structural studies, using small angle X-ray scattering and molecular dynamic simulations, allows us to understand the behavior of transferrin on a molecular level.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2019.100017","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137264","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 10

Structural insights into human Arginase-1 pH dependence and its inhibition by the small molecule inhibitor CB-1158 人精氨酸酶-1 pH依赖性的结构研究及其小分子抑制剂CB-1158的抑制作用

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2019.100014

Yvonne Grobben, Joost C.M. Uitdehaag, Nicole Willemsen-Seegers, Werner W.A. Tabak, Jos de Man, Rogier C. Buijsman, Guido J.R. Zaman

{"title":"Structural insights into human Arginase-1 pH dependence and its inhibition by the small molecule inhibitor CB-1158","authors":"Yvonne Grobben, Joost C.M. Uitdehaag, Nicole Willemsen-Seegers, Werner W.A. Tabak, Jos de Man, Rogier C. Buijsman, Guido J.R. Zaman","doi":"10.1016/j.yjsbx.2019.100014","DOIUrl":"10.1016/j.yjsbx.2019.100014","url":null,"abstract":"<div><p>Arginase-1 is a manganese-dependent metalloenzyme that catalyzes the hydrolysis of L-arginine into L-ornithine and urea. Arginase-1 is abundantly expressed by tumor-infiltrating myeloid cells that promote tumor immunosuppression, which is relieved by inhibition of Arginase-1. We have characterized the potencies of the Arginase-1 reference inhibitors (2<em>S</em>)-2-amino-6-boronohexanoic acid (ABH) and <em>N</em><sup>ω</sup>-hydroxy-nor-L-arginine (nor-NOHA), and studied their pH-dependence and binding kinetics. To gain a better understanding of the structural changes underlying the high pH optimum of Arginase-1 and its pH-dependent inhibition, we determined the crystal structure of the human Arginase-1/ABH complex at pH 7.0 and 9.0. These structures revealed that at increased pH, the manganese cluster assumes a more symmetrical coordination structure, which presumably contributes to its increase in catalytic activity. Furthermore, we show that binding of ABH involves the presence of a sodium ion close to the manganese cluster. We also studied the investigational new drug CB-1158 (INCB001158). This inhibitor has a low-nanomolar potency at pH 7.4 and increases the thermal stability of Arginase-1 more than ABH and nor-NOHA. Moreover, CB-1158 displays slow association and dissociation kinetics at both pH 9.5 and 7.4, as indicated by surface plasmon resonance. The potent character of CB-1158 is presumably due to its increased rigidity compared to ABH as well as the formation of an additional hydrogen-bond network as observed by resolution of the Arginase-1/CB-1158 crystal structure.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2019.100014","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137863","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 25

High resolution CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis 结核分枝杆菌环状毒力因子EspB的高分辨率CryoEM结构

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100029

Jérémie Piton , Florence Pojer , Soichi Wakatsuki , Cornelius Gati , Stewart T. Cole

{"title":"High resolution CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis","authors":"Jérémie Piton , Florence Pojer , Soichi Wakatsuki , Cornelius Gati , Stewart T. Cole","doi":"10.1016/j.yjsbx.2020.100029","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2020.100029","url":null,"abstract":"<div><p>The EspB protein of <em>Mycobacterium tuberculosis</em> is a 60 kDa virulence factor, implicated in conjugation and exported by the ESX-1 system of which it may also be a component. Previous attempts to obtain high-resolution maps of EspB by cryo-electron microscopic examination of single particles have been thwarted by severe orientation bias of the particles. This was overcome by using detergent as a surfactant thereby allowing reconstruction of the EspB structure at 3.37 Å resolution. The final structure revealed the N-terminal domain of EspB to be organized as a cylindrical heptamer with dimensions of 90 Å x 90 Å and a central channel of 45 Å diameter whereas the C-terminal domain was unstructured. New atomic insight was obtained into the helical packing required for protomer interactions and the overall electrostatic potential. The external surface is electronegatively charged while the channel is lined with electropositive patches. EspB thus has many features of a pore-like transport protein that might allow the passage of an ESX-1 substrate such as the 35 Å diameter EsxA-EsxB heterodimer or B-form DNA consistent with its proposed role in DNA uptake.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100029","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72076018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 17

In crystallo-screening for discovery of human norovirus 3C-like protease inhibitors 人诺如病毒3C样蛋白酶抑制剂的晶体内筛选

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100031

Jingxu Guo , Alice Douangamath , Weixiao Song , Alun R. Coker , A.W. Edith Chan , Steve P. Wood , Jonathan B. Cooper , Efrat Resnick , Nir London , Frank von Delft

{"title":"In crystallo-screening for discovery of human norovirus 3C-like protease inhibitors","authors":"Jingxu Guo , Alice Douangamath , Weixiao Song , Alun R. Coker , A.W. Edith Chan , Steve P. Wood , Jonathan B. Cooper , Efrat Resnick , Nir London , Frank von Delft","doi":"10.1016/j.yjsbx.2020.100031","DOIUrl":"https://doi.org/10.1016/j.yjsbx.2020.100031","url":null,"abstract":"<div><p>Outbreaks of human epidemic nonbacterial gastroenteritis are mainly caused by noroviruses. Viral replication requires a 3C-like cysteine protease (3CL<sup>pro</sup>) which processes the 200 kDa viral polyprotein into six functional proteins. The 3CL<sup>pro</sup> has attracted much interest due to its potential as a target for antiviral drugs. A system for growing high-quality crystals of native Southampton norovirus 3CL<sup>pro</sup> (SV3CP) has been established, allowing the ligand-free crystal structure to be determined to 1.3 Å in a tetrameric state. This also allowed crystal-based fragment screening to be performed with various compound libraries, ultimately to guide drug discovery for SV3CP. A total of 19 fragments were found to bind to the protease out of the 844 which were screened. Two of the hits were located at the active site of SV3CP and showed good inhibitory activity in kinetic assays. Another 5 were found at the enzyme’s putative RNA-binding site and a further 11 were located in the symmetric central cavity of the tetramer.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100031","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72076019","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

A guided approach for subtomogram averaging of challenging macromolecular assemblies 具有挑战性的大分子组合的亚层析图平均的引导方法

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100041

Benjamin Basanta , Saikat Chowdhury , Gabriel C. Lander , Danielle A. Grotjahn

引用次数: 7

Structures and dynamics of the novel S1/S2 protease cleavage site loop of the SARS-CoV-2 spike glycoprotein 新型SARS-CoV-2刺突糖蛋白S1/S2蛋白酶裂解位点环的结构和动力学

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100038

Thomas Lemmin , David Kalbermatter , Daniel Harder , Philippe Plattet , Dimitrios Fotiadis

{"title":"Structures and dynamics of the novel S1/S2 protease cleavage site loop of the SARS-CoV-2 spike glycoprotein","authors":"Thomas Lemmin , David Kalbermatter , Daniel Harder , Philippe Plattet , Dimitrios Fotiadis","doi":"10.1016/j.yjsbx.2020.100038","DOIUrl":"10.1016/j.yjsbx.2020.100038","url":null,"abstract":"<div><p>At the end of 2019, a new highly virulent coronavirus known under the name SARS-CoV-2 emerged as a human pathogen. One key feature of SARS-CoV-2 is the presence of an enigmatic insertion in the spike glycoprotein gene representing a novel multibasic S1/S2 protease cleavage site. The proteolytic cleavage of the spike at this site is essential for viral entry into host cells. However, it has been systematically abrogated in structural studies in order to stabilize the spike in the prefusion state. In this study, multi-microsecond molecular dynamics simulations and <em>ab initio</em> modeling were leveraged to gain insights into the structures and dynamics of the loop containing the S1/S2 protease cleavage site. They unveiled distinct conformations, formations of short helices and interactions of the loop with neighboring glycans that could potentially regulate the accessibility of the cleavage site to proteases and its processing. In most conformations, this loop protrudes from the spike, thus representing an attractive SARS-CoV-2 specific therapeutic target.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100038","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38476957","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 37

SIMPLE 3.0. Stream single-particle cryo-EM analysis in real time 简单的3.0。实时流单粒子低温电镜分析

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100040

Joseph Caesar , Cyril F. Reboul , Chiara Machello , Simon Kiesewetter , Molly L. Tang , Justin C. Deme , Steven Johnson , Dominika Elmlund , Susan M. Lea , Hans Elmlund

{"title":"SIMPLE 3.0. Stream single-particle cryo-EM analysis in real time","authors":"Joseph Caesar , Cyril F. Reboul , Chiara Machello , Simon Kiesewetter , Molly L. Tang , Justin C. Deme , Steven Johnson , Dominika Elmlund , Susan M. Lea , Hans Elmlund","doi":"10.1016/j.yjsbx.2020.100040","DOIUrl":"10.1016/j.yjsbx.2020.100040","url":null,"abstract":"<div><p>We here introduce the third major release of the SIMPLE (Single-particle IMage Processing Linux Engine) open-source software package for analysis of cryogenic transmission electron microscopy (cryo-EM) movies of single-particles (Single-Particle Analysis, SPA). Development of SIMPLE 3.0 has been focused on real-time data processing using minimal CPU computing resources to allow easy and cost-efficient scaling of processing as data rates escalate. Our stream SPA tool implements the steps of anisotropic motion correction and CTF estimation, rapid template-based particle identification and 2D clustering with automatic class rejection. SIMPLE 3.0 additionally features an easy-to-use web-based graphical user interface (GUI) that can be run on any device (workstation, laptop, tablet or phone) and supports a remote multi-user environment over the network. The new project-based execution model automatically records the executed workflow and represents it as a flow diagram in the GUI. This facilitates meta-data handling and greatly simplifies usage. Using SIMPLE 3.0, it is possible to automatically obtain a clean SP data set amenable to high-resolution 3D reconstruction directly upon completion of the data acquisition, without the need for extensive image processing post collection. Only minimal standard CPU computing resources are required to keep up with a rate of ∼300 Gatan K3 direct electron detector movies per hour. SIMPLE 3.0 is available for download from simplecryoem.com.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100040","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38351940","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 8

A complex between the Zika virion and the Fab of a broadly cross-reactive neutralizing monoclonal antibody revealed by cryo-EM and single particle analysis at 4.1 Å resolution 通过低温电镜和单颗粒分析，以4.1 Å分辨率发现了寨卡病毒粒子和广泛交叉反应中和单克隆抗体Fab之间的复合物

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100028

Anu Tyagi , Tofayel Ahmed , Jian Shi , Shashi Bhushan

{"title":"A complex between the Zika virion and the Fab of a broadly cross-reactive neutralizing monoclonal antibody revealed by cryo-EM and single particle analysis at 4.1 Å resolution","authors":"Anu Tyagi , Tofayel Ahmed , Jian Shi , Shashi Bhushan","doi":"10.1016/j.yjsbx.2020.100028","DOIUrl":"10.1016/j.yjsbx.2020.100028","url":null,"abstract":"<div><p>Zika virus (ZIKV) recently emerged as a major public health concern because it can cause fetal microcephaly and neurological disease such as the Guillain-Barré syndrome. A particularly potent class of broadly neutralizing antibodies (nAbs) targets a quaternary epitope located at the interface of two envelope proteins monomers, exposed at the surface of the mature virion. This “E-dimer-dependent epitope” (EDE), comprises the fusion loop of one monomer at the tip of domain II of E and a portion of the domains I and III of the adjacent monomer. Since this epitope largely overlaps with the binding site of the precursor membrane protein (prM) during Zika virion maturation, its molecular surface is evolutionary conserved in flaviviruses such as Dengue and Zika viruses, and can elicit antibodies that broadly neutralize various ZIKV strains. Here, we present a cryo-EM reconstruction at 4.1 Å resolution of the virion bound to the antigen binding fragment (Fab) of an antibody that targets this mutationally-constrained quaternary epitope. The Fab incompletely covers the surface of the virion as it does not bind next to its 5-fold icosahedral axes. The structure reveals details of the binding mode of this potent neutralizing class of antibodies and can inform the design of immunogens and vaccines targeting this conserved epitope.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100028","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38137190","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 5

Specificity in PDZ-peptide interaction networks: Computational analysis and review pdz -肽相互作用网络的特异性:计算分析和回顾

IF 2.9

Journal of Structural Biology: X Pub Date : 2020-01-01 DOI: 10.1016/j.yjsbx.2020.100022

Jeanine F. Amacher , Lionel Brooks 3rd , Thomas H. Hampton , Dean R. Madden

{"title":"Specificity in PDZ-peptide interaction networks: Computational analysis and review","authors":"Jeanine F. Amacher , Lionel Brooks 3rd , Thomas H. Hampton , Dean R. Madden","doi":"10.1016/j.yjsbx.2020.100022","DOIUrl":"10.1016/j.yjsbx.2020.100022","url":null,"abstract":"<div><p>Globular PDZ domains typically serve as protein–protein interaction modules that regulate a wide variety of cellular functions via recognition of short linear motifs (SLiMs). Often, PDZ mediated-interactions are essential components of macromolecular complexes, and disruption affects the entire scaffold. Due to their roles as linchpins in trafficking and signaling pathways, PDZ domains are attractive targets: both for controlling viral pathogens, which bind PDZ domains and hijack cellular machinery, as well as for developing therapies to combat human disease. However, successful therapeutic interventions that avoid off-target effects are a challenge, because each PDZ domain interacts with a number of cellular targets, and specific binding preferences can be difficult to decipher. Over twenty-five years of research has produced a wealth of data on the stereochemical preferences of individual PDZ proteins and their binding partners. Currently the field lacks a central repository for this information. Here, we provide this important resource and provide a manually curated, comprehensive list of the 271 human PDZ domains. We use individual domain, as well as recent genomic and proteomic, data in order to gain a holistic view of PDZ domains and interaction networks, arguing this knowledge is critical to optimize targeting selectivity and to benefit human health.</p></div>","PeriodicalId":17238,"journal":{"name":"Journal of Structural Biology: X","volume":null,"pages":null},"PeriodicalIF":2.9,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.yjsbx.2020.100022","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37833891","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 30