Biomolecular NMR Assignments最新文献

1H, 13C, and 15N resonance assignments and solution structure of the first double-stranded RNA-binding domain of DExH-Box Helicase 30 (DHX30) DExH-Box解旋酶30 （DHX30）第一双链rna结合域的1H、13C和15N共振分配和溶液结构

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-10-09 DOI: 10.1007/s12104-026-10279-0

Chikage Abe, Yutaka Muto, Fahu He, Mari Takahashi, Kengo Tsuda, Takashi Nagata, Akiko Tanaka, Naohiro Kobayashi, Takanori Kigawa, Peter Güntert, Mikako Shirouzu, Shigeyuki Yokoyama, Kanako Kuwasako

{"title":"1H, 13C, and 15N resonance assignments and solution structure of the first double-stranded RNA-binding domain of DExH-Box Helicase 30 (DHX30)","authors":"Chikage Abe, Yutaka Muto, Fahu He, Mari Takahashi, Kengo Tsuda, Takashi Nagata, Akiko Tanaka, Naohiro Kobayashi, Takanori Kigawa, Peter Güntert, Mikako Shirouzu, Shigeyuki Yokoyama, Kanako Kuwasako","doi":"10.1007/s12104-026-10279-0","DOIUrl":"10.1007/s12104-026-10279-0","url":null,"abstract":"<div><p>DHX30 is a member of the DExH-box helicase family and contains two double-stranded RNA-binding domains (dsRBDs) N-terminal to the helicase core domain. DHX30 plays a fundamental role in regulating the translation of transcripts encoding mitoribosomal proteins, thereby facilitating mitoribosome biogenesis. Additionally, DHX30 is involved in the formation of stress granules. These intracellular structures are composed of proteins and RNAs, including mRNAs, and form under stress conditions in association with translational repression. Recent studies have demonstrated that pathogenic mutations in DHX30 underlie a severe neurodevelopmental disorder termed neurodevelopmental disorder with variable motor and language impairment (NEDMIAL), possibly in part through aberrant stress-granule formation. Structural characterization of these RNA-binding domains is an important step toward understanding the molecular basis of DHX30 function. In this study, we focus on the first dsRBD (dsRBD-1) of human DHX30 and report its <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N resonance assignments and solution structure. DHX30 dsRBD-1 adopts an α0–α1–α1′–β1–β2–β3–α2–α3 topology, with three additional helices (α0, α1′, and α3) relative to the canonical dsRBD topology (α1–β1–β2–β3–α2). To our knowledge, this is the first experimentally determined structure of a DHX30 domain. These resonance assignments and structural insights provide a valuable foundation for future structural and functional studies of DHX30.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149132795","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Backbone and side chain 1H, 13C and 15N chemical shift assignment of the cargo-recognition domain MOTH of human TANGO1 人类tango - 1的主侧链1H， 13C和15N的化学位移分配

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-09-11 DOI: 10.1007/s12104-026-10278-1

Jelena Auch, Anna Carlotta Peddinghaus, Raphael Stoll

{"title":"Backbone and side chain 1H, 13C and 15N chemical shift assignment of the cargo-recognition domain MOTH of human TANGO1","authors":"Jelena Auch, Anna Carlotta Peddinghaus, Raphael Stoll","doi":"10.1007/s12104-026-10278-1","DOIUrl":"10.1007/s12104-026-10278-1","url":null,"abstract":"<div><p>The cellular export of large-sized proteins, such as collagen or fibrillin, necessitates a specialized transport pathway tailored towards their size. For collagen and possibly also other bulky proteins, the Transport ANd Golgi Organization 1 (TANGO1) protein plays a substantial role in the transfer from the Endoplasmic Reticulum (ER) to the Golgi apparatus. TANGO1 and related proteins organize the ER exit sites and generate large export structures within the cytosol while anchored to the ER membrane. In contrast to other proteins involved, TANGO1 features a folded domain in the ER lumen, which seems to be central for detecting cargos. This cargo-recognition domain has been shown to bind the collagen-specific chaperone HSP47 (Ishikawa et al. 2016) as well as type IV collagen directly (Arnolds and Stoll 2023). However, the exact molecular mechanism of these interactions remains unknown. The resonance assignments presented here lay the foundation for the experiments studying the binding process on a molecular level and is designed to facilitate investigations into how TANGO1 detects and selects the cargos to be exported.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10278-1.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148927861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The 1H, 15N and 13C backbone resonance assignments of an intrinsically disordered region (467–696) of breast cancer type 1 susceptibility protein (BRCA1) 乳腺癌1型易感蛋白（BRCA1）内在无序区（467-696）的1H， 15N和13C骨干共振分配

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-09-04 DOI: 10.1007/s12104-026-10277-2

Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich

{"title":"The 1H, 15N and 13C backbone resonance assignments of an intrinsically disordered region (467–696) of breast cancer type 1 susceptibility protein (BRCA1)","authors":"Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich","doi":"10.1007/s12104-026-10277-2","DOIUrl":"10.1007/s12104-026-10277-2","url":null,"abstract":"<div><p>The tumor suppressor protein breast cancer type 1 susceptibility protein (BRCA1) plays a central role in maintaining genome stability through its involvement in DNA damage repair, transcriptional regulation, and cell-cycle control. BRCA1 functions as an obligate heterodimer with its binding partner, the BRCA1-associated RING domain protein 1 (BARD1), to coordinate accurate DNA repair. While the structured N- and C-terminal domains of BRCA1 have been well-characterized, the large central region encoded largely by exon 11 that comprises ~ 80% of the protein, is intrinsically disordered, and remains poorly structurally characterized. This intrinsically disordered region (IDR) harbors critical interaction interfaces for key proteins involved in genome maintenance, including RAD50, RAD51, MYC, and RB. Here, we report the backbone resonance assignments of a BRCA1 IDR construct spanning residues 467–696, providing a foundation for future studies aimed at understanding how the disordered central region of BRCA1 contributes to homologous recombination, interactions with BARD1, and overall BRCA1 tumor suppressor function.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13541922/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148885922","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The1H, 15N and13C backbone resonance assignments of an intrinsically disordered region (124–270) of BRCA1 associated RING domain 1 (BARD1) BRCA1相关环结构域1 （BARD1）的内在无序区（124-270）的1h， 15N和13c骨干共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-09-01 DOI: 10.1007/s12104-026-10276-3

Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich

{"title":"The1H, 15N and13C backbone resonance assignments of an intrinsically disordered region (124–270) of BRCA1 associated RING domain 1 (BARD1)","authors":"Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich","doi":"10.1007/s12104-026-10276-3","DOIUrl":"10.1007/s12104-026-10276-3","url":null,"abstract":"<div><p>The BRCA1-associated RING domain protein 1 (BARD1) is the obligate binding partner of the tumor suppressor breast cancer type 1 susceptibility protein (BRCA1) and plays a critical role in maintaining genome integrity. BARD1 contains structured N- and C-terminal domains that mediate heterodimerization with BRCA1, recognition of chromatin marks, and DNA repair functions. Approximately 40% of BARD1 is intrinsically disordered, particularly in the central region of the protein. This intrinsically disordered region (IDR) engages DNA and key repair proteins such as RAD51, BLM, and WRN. DNA binding through the BARD1 IDR facilitates H2A ubiquitination by the BRCA1-BARD1 complex and is essential for stimulating long-range DNA end resection during homologous recombination, underscoring its role in accurate DNA repair. Despite these insights, structural characterization of the IDR remains limited, leaving questions regarding its functional interplay with BRCA1 and other repair factors unresolved. Here, we report the backbone resonance assignments of a BARD1 IDR construct spanning residues 124–270, providing a foundation for future studies aimed at understanding how the disordered regions of BARD1 interact with various binding partners, and cooperates with itself and BRCA1 to regulate genome stability.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13534175/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148872437","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

1H, 13C, and 15N backbone and side-chain resonance assignments of the Nostoc sp. H-NOX C139A variant in complex with the soluble Guanylyl Cyclase inhibitor Zinc Protoporphyrin IX Nostoc sp. H-NOX C139A突变体与可溶性环化酶抑制剂锌原卟啉IX配合物的1H， 13C和15N主链和侧链共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-08-26 DOI: 10.1007/s12104-026-10274-5

Stefanos I. Gravalos, Emmanouil N. Andreadis, Francesca Cantini, Lucia Banci, Georgios A. Spyroulias

{"title":"1H, 13C, and 15N backbone and side-chain resonance assignments of the Nostoc sp. H-NOX C139A variant in complex with the soluble Guanylyl Cyclase inhibitor Zinc Protoporphyrin IX","authors":"Stefanos I. Gravalos, Emmanouil N. Andreadis, Francesca Cantini, Lucia Banci, Georgios A. Spyroulias","doi":"10.1007/s12104-026-10274-5","DOIUrl":"10.1007/s12104-026-10274-5","url":null,"abstract":"<div><p>The H-NOX (Heme–Nitric oxide/Oxygen binding) domain is highly conserved among both eukaryotes and bacteria. In human soluble Guanylyl Cyclase (sGC), the H-NOX domain functions as a sensor for the gaseous signaling molecule Nitric Oxide (NO). Located at the N-terminus of the enzyme, the heme B-binding H-NOX domain regulates the catalytic domain at the C-terminus, which catalyzes the conversion of GTP (guanosine 5′-triphosphate) to cGMP (cyclic Guanosine MonoPhosphate). The present study employs the bacterial homolog <i>Nostoc sp.</i> H-NOX (<i>Ns</i> H-NOX) C139A mutant together with the sGC inhibitor Zinc Protoporphyrin IX (ZnPPIX) as experimental tools to investigate the still poorly understood mechanisms underlying sGC activation and inhibition, and to elucidate either the chemical features of novel scaffolds associated with a new class of activators, or the distinct activities imposed by two prosthetic groups sharing the same organic framework, but differing in the chelated transition metal. Here, we present the conditions employed for the formation of the complex between the <i>Ns</i> H-NOX C139A mutant and the sGC inhibitor ZnPPIX, together with the UV–Vis absorption spectra of the heme-bound and ZnPPIX-bound protein forms. Furthermore, we report the NMR backbone and side-chain resonance assignments (<sup>1</sup>H, <sup>13</sup>C, <sup>15</sup>N) of the complex, as well as the chemical shift-based secondary structure predictions. These data will be used for comparative analysis of <sup>15</sup>N NMR relaxation experiments in the basal, fully active and inactive H-NOX states, aiming to elucidate the role of Η-ΝΟΧ protein dynamics in the initiation and propagation of sGC activation signal.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10274-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148817014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

1H, 15N and 13C backbone and side-chain resonance assignments of Amblyomin-X Kunitz domain Amblyomin-X Kunitz结构域的1H， 15N和13C主链和侧链共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-08-24 DOI: 10.1007/s12104-026-10275-4

Vitor S. Almeida, Virginnia C. Nogueira, Livia S. O. Conti, Ana Paula B. Costa, Ana Paula Valente

{"title":"1H, 15N and 13C backbone and side-chain resonance assignments of Amblyomin-X Kunitz domain","authors":"Vitor S. Almeida, Virginnia C. Nogueira, Livia S. O. Conti, Ana Paula B. Costa, Ana Paula Valente","doi":"10.1007/s12104-026-10275-4","DOIUrl":"10.1007/s12104-026-10275-4","url":null,"abstract":"<div><p>Amblyomin-X is a Kunitz-type inhibitor of factor Xa (FXa) from the tick <i>Amblyomma sculptum</i> with promising anticoagulant activity and potential therapeutic applications. Despite the relevance, the molecular basis of its interaction with FXa remains poorly understood, limiting a detailed understanding of its mechanism of action. In this study, we report the <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N resonance assignments of the Amblyomin-X Kunitz domain obtained by multidimensional NMR spectroscopy. High-quality spectra enabled extensive assignment, reaching 97.9% completeness for backbone assignments and 79.8% for side-chain assignments. The <sup>1</sup>H-<sup>15</sup>N HSQC spectrum shows excellent signal dispersion, consistent with a well-folded protein in solution. Furthermore, chemical shift-based structure analysis reveals elements that agree with the canonical Kunitz fold, including characteristic β-strands and helical regions. These results provide the first detailed NMR characterization of the Amblyomin-X Kunitz domain l. The resonance assignments presented here constitute a critical foundation for future structural and dynamical studies, including analyses of protein-ligand interactions. Ultimately, this work contributes to a deeper understanding of the molecular determinants governing FXa inhibition by Amblyomin-X and supports ongoing efforts to develop novel anticoagulant strategies based on Kunitz-type inhibitors.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13503397/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148811778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

1H, 15N, 13C backbone resonance assignment of Escherichia coli AlkB in complex with Zn(II) and α-ketoglutarate 大肠杆菌AlkB与Zn（II）和α-酮戊二酸配合物的1H， 15N， 13C骨干共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-07-14 DOI: 10.1007/s12104-026-10273-6

Sayan Das, Jeffrey A. Purslow, Kyle Malcom, Joshua Knott, Vincenzo Venditti

{"title":"1H, 15N, 13C backbone resonance assignment of Escherichia coli AlkB in complex with Zn(II) and α-ketoglutarate","authors":"Sayan Das, Jeffrey A. Purslow, Kyle Malcom, Joshua Knott, Vincenzo Venditti","doi":"10.1007/s12104-026-10273-6","DOIUrl":"10.1007/s12104-026-10273-6","url":null,"abstract":"<div><p>Protein and nucleic acid alkylation are important genetic and epigenetic modifications. The dynamic balance between alkylation and dealkylation is regulated by distinct sets of enzymes and is essential for maintaining genomic stability. <i>Escherichia coli</i> AlkB is a member of the Alkylation B (AlkB) family of dioxygenases that dealkylates a wide range of nucleic acid substrates in <i>E. coli</i>, thereby playing a crucial role in cellular repair processes and epigenetic regulation. Here, we report the backbone <sup>1</sup>H, <sup>15</sup>N, <sup>13</sup>C chemical shift assignment of <i>E. coli</i> AlkB in complex with Zn<sup>2+</sup> and α-ketoglutarate. Experiments were acquired at 20 °C by heteronuclear multidimensional NMR spectroscopy. Collectively, 91% of all <sup>13</sup>C, <sup>15</sup>N and <sup>1</sup>H backbone resonances of Alkb were assigned, with 182 out of a possible 200 residues assigned in the <sup>1</sup>H–<sup>15</sup>N TROSY spectrum. Using the program TALOS + , a secondary structure prediction was generated from the assigned backbone resonances that is consistent with the previously reported X-ray structure of the enzyme. The reported assignment will permit investigations of the protein structural dynamics anticipated to provide crucial insight regarding fundamental aspects in the recognition and enzyme regulation processes.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-07-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10273-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148434725","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

1H, 15N and 13C resonance assignment of caspase recruitment domain of death receptor 6 死亡受体caspase募集结构域的1H， 15N和13C共振分配

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-07-11 DOI: 10.1007/s12104-026-10272-7

Biao Xia, Yajing Duan, Yuzhe Ning, Wensu Yuan, Zhi Lin, Zhen Li

引用次数: 0

NMR resonance assignments (¹H, ¹³C, ¹⁵N) of jararacin (rJarc), a disintegrin from Bothrops jararaca jararacin （rJarc）的核磁共振赋值（¹H，¹³C，¹5 N）。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-06-15 DOI: 10.1007/s12104-026-10271-8

Jorge Eduardo Chang Estrada, Ariana Azevedo Vasconcelos, Russolina Benedeta Zingali, Fabio C. L. Almeida

引用次数: 0

NMR study of human macroPARPs domains: 1H, 13C and 15N backbone and side-chain chemical shift assignments of hPARP9 macro domain 1 (MD1) in the apo and in the ADPr bound states 人类macroPARPs结构域的核磁共振研究：hPARP9宏结构域1 （MD1）在载子和ADPr结合态的1H， 13C和15N主链和侧链化学位移分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-06-12 DOI: 10.1007/s12104-026-10270-9

Danai Moschidi, Nikolaos K. Fourkiotis, Sofia-Antigoni Tsatsouli, Aikaterini C. Tsika, Georgios A. Spyroulias

{"title":"NMR study of human macroPARPs domains: 1H, 13C and 15N backbone and side-chain chemical shift assignments of hPARP9 macro domain 1 (MD1) in the apo and in the ADPr bound states","authors":"Danai Moschidi, Nikolaos K. Fourkiotis, Sofia-Antigoni Tsatsouli, Aikaterini C. Tsika, Georgios A. Spyroulias","doi":"10.1007/s12104-026-10270-9","DOIUrl":"10.1007/s12104-026-10270-9","url":null,"abstract":"<div><p>ADP-ribosylation is a reversible post-translational modification that regulates diverse cellular processes, including DNA damage repair, transcription, cell proliferation and innate immune responses, and is primarily catalyzed by members of the PARP family. While all 17 human PARPs contain a conserved C-terminal ADP-ribosyltransferase (ART) domain, only catalytically active members transfer ADP-ribose (ADPr) from nicotinamide adenine dinucleotide (NAD⁺) onto proteins or nucleic acids, and their N-terminal accessory domains, such as macro domains (MDs), WWE domains or RNA-binding motifs, mediate interactions that diversify PARP functions. Human PARP9 (hPARP9), known also as BAL1, is catalytically inactive due to sequence variations in catalytically important residues in the ART domain, but plays crucial roles in antiviral and antibacterial defense, stress responses and tumor progression through its heterodimeric interaction with the E3 ubiquitin ligase DTX3L. hPARP9 contains two tandem MDs (MD1 and MD2), with MD1 acting as a MacroD-type hydrolase “eraser” of mono-ADP-ribosylation (MARylation), while MD2 functions as an ADPr “reader”. Their different role in the ADP-ribosylation pathway highlights the importance of structural and functional characterization for understanding ADPr-mediated cellular signaling. In this study, we report the NMR backbone and side-chain resonance assignments of hPARP9 MD1 in both apo and ADPr bound states. In addition, the secondary structure predictions using TALOS+ server and the Chemical Shift Perturbation (CSP) analysis upon ADPr binding are presented. The latter illustrates the MD substrate’s accommodation mode and identifies the residues involved in ADPr binding, thus related to MDs’ hydrolytic activity.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.6,"publicationDate":"2026-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10270-9.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148222266","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0