Biomolecular NMR Assignments最新文献_第10页

1H, 13C, 15N Backbone and sidechain chemical shift assignments of the C-terminal domain of human UDP-glucuronosyltransferase 2B17 (UGT2B17-C) 人udp -葡萄糖醛酸基转移酶2B17 (UGT2B17-C) c端结构域的1H, 13C, 15N主链和侧链化学位移定位

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-02-09 DOI: 10.1007/s12104-023-10122-w

Anamika Sulekha, Michael J. Osborne, Jadwiga Gasiorek, Katherine L. B. Borden

{"title":"1H, 13C, 15N Backbone and sidechain chemical shift assignments of the C-terminal domain of human UDP-glucuronosyltransferase 2B17 (UGT2B17-C)","authors":"Anamika Sulekha, Michael J. Osborne, Jadwiga Gasiorek, Katherine L. B. Borden","doi":"10.1007/s12104-023-10122-w","DOIUrl":"10.1007/s12104-023-10122-w","url":null,"abstract":"<div><p>UDP-glucuronosyltransferases are the principal enzymes involved in the glucuronidation of metabolites and xenobiotics for physiological clearance in humans. Though glucuronidation is an indispensable process in the phase II metabolic pathway, UGT-mediated glucuronidation of most prescribed drugs (> 55%) and clinical evidence of UGT-associated drug resistance are major concerns for therapeutic development. While UGTs are highly conserved enzymes, they manifest unique substrate and inhibitor specificity which is poorly understood given the dearth of experimentally determined full-length structures. Such information is important not only to conceptualize their specificity but is central to the design of inhibitors specific to a given UGT in order to avoid toxicity associated with pan-UGT inhibitors. Here, we provide the <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone (~ 90%) and sidechain (~ 62%) assignments for the C-terminal domain of UGT2B17, which can be used to determine the molecular binding sites of inhibitor and substrate, and to understand the atomic basis for inhibitor selectivity between UGT2B17 and other members of the UGT2B subfamily. Given the physiological relevance of UGT2B17 in the elimination of hormone-based cancer drugs, these assignments will contribute towards dissecting the structural basis for substrate specificity, selective inhibitor recognition and other aspects of enzyme activity with the goal of selectively overcoming glucuronidation-based drug resistance.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"67 - 73"},"PeriodicalIF":0.9,"publicationDate":"2023-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4382835","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: 1

Backbone NMR resonance assignment of the apo human Tsg101-UEV domain 载子人Tsg101-UEV结构域的主核磁共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-02-06 DOI: 10.1007/s12104-023-10119-5

Danai Moschidi, François-Xavier Cantrelle, Emmanuelle Boll, Xavier Hanoulle

{"title":"Backbone NMR resonance assignment of the apo human Tsg101-UEV domain","authors":"Danai Moschidi, François-Xavier Cantrelle, Emmanuelle Boll, Xavier Hanoulle","doi":"10.1007/s12104-023-10119-5","DOIUrl":"10.1007/s12104-023-10119-5","url":null,"abstract":"<div><p>The Endosomal Sorting Complex Required for Transport (ESCRT) pathway, through inverse topology membrane remodeling, is involved in many biological functions, such as ubiquitinated membrane receptor trafficking and degradation, multivesicular bodies (MVB) formation and cytokinesis. Dysfunctions in ESCRT pathway have been associated to several human pathologies, such as cancers and neurodegenerative diseases. The ESCRT machinery is also hijacked by many enveloped viruses to bud away from the plasma membrane of infected cells. Human tumor susceptibility gene 101 (Tsg101) protein is an important ESCRT-I complex component. The structure of the N-terminal ubiquitin E2 variant (UEV) domain of Tsg101 (Tsg101-UEV) comprises an ubiquitin binding pocket next to a late domain [P(S/T)AP] binding groove. These two binding sites have been shown to be involved both in the physiological roles of ESCRT-I and in the release of the viral particles, and thus are attractive targets for antivirals. The structure of the Tsg101-UEV domain has been characterized, using X-ray crystallography or NMR spectroscopy, either in its apo-state or bound to ubiquitin or late domains. In this study, we report the backbone NMR resonance assignments, including the proline signals, of the apo human Tsg101-UEV domain, that so far was not publicly available. These data, that are in good agreement with the crystallographic structure of Tsg101-UEV domain, can therefore be used for further NMR studies, including protein-protein interaction studies and drug discovery.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"49 - 54"},"PeriodicalIF":0.9,"publicationDate":"2023-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4246206","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

Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor NMDA受体glun1c0结构域(残基841-865)上钙调蛋白的化学移位配位

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-02-05 DOI: 10.1007/s12104-023-10121-x

Aritra Bej, James B. Ames

引用次数: 2

1H, 15N and 13C resonance assignments of a minimal CPSF73-CPSF100 C-terminal heterodimer 最小CPSF73-CPSF100 c端异二聚体的1H, 15N和13C共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-02-01 DOI: 10.1007/s12104-023-10118-6

Stéphane Thore, Sébastien Fribourg, Cameron D. Mackereth

引用次数: 1

The 1H, 15N and 13C resonance assignments of dengue virus capsid protein with the deletion of the intrinsically disordered N-terminal region 登革病毒衣壳蛋白内在无序n端缺失的1H、15N和13C共振配位

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-02-01 DOI: 10.1007/s12104-022-10115-1

Glauce M. Barbosa, Maria A. Morando, Andrea T. Da Poian, Fabio C. L. Almeida

引用次数: 0

1H, 15N, 13C backbone and sidechain resonance assignments and secondary structure of mouse NOTCH1 EGF27 小鼠NOTCH1 EGF27的1H, 15N, 13C骨干和侧链共振分配和二级结构

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2022-12-24 DOI: 10.1007/s12104-022-10116-0

Justin A. Grennell, Kendra D. Jenkins, Kelvin B. Luther, John Glushka, Robert S. Haltiwanger, Megan A. Macnaughtan

{"title":"1H, 15N, 13C backbone and sidechain resonance assignments and secondary structure of mouse NOTCH1 EGF27","authors":"Justin A. Grennell, Kendra D. Jenkins, Kelvin B. Luther, John Glushka, Robert S. Haltiwanger, Megan A. Macnaughtan","doi":"10.1007/s12104-022-10116-0","DOIUrl":"10.1007/s12104-022-10116-0","url":null,"abstract":"<div><p>NOTCH1 is a transmembrane receptor in metazoans that is linked to a variety of disorders. The receptor contains an extracellular domain (ECD) with 36 tandem epidermal growth factor-like (EGF) repeats. The ECD is responsible for intercellular signaling via protein–ligand interactions with neighboring cells. Each EGF repeat consists of approximately 40 amino acids and 3 conserved disulfide bonds. The <i>Abruptex</i> region (EGF24-29) is critical for NOTCH1 signaling and is known for its missense mutations. Certain EGF repeats are modified with the addition of <i>O</i>-linked glycans and many have calcium binding sites, which give each EGF repeat a unique function. It has been shown that the loss of the <i>O</i>-fucose site of EGF27 alters NOTCH1 activity. To investigate the role of glycosylation in the NOTCH1 signaling pathway, nuclear magnetic resonance spectroscopy has been employed to study the structures of EGF27 and its glycoforms. Here, we report the backbone and sidechain <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C-resonance assignments of the unmodified EGF27 protein and the predicted secondary structure derived from the assigned chemical shifts.\u0000</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"27 - 35"},"PeriodicalIF":0.9,"publicationDate":"2022-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-022-10116-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"5259852","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 assignments of the mRNA binding protein hnRNP A18 mRNA结合蛋白hnRNP A18的1H, 13C和15N分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2022-12-21 DOI: 10.1007/s12104-022-10117-z

Katherine M. Coburn, Braden Roth, Kristen M. Varney, France Carrier, David J. Weber

{"title":"1H, 13C, and 15N assignments of the mRNA binding protein hnRNP A18","authors":"Katherine M. Coburn, Braden Roth, Kristen M. Varney, France Carrier, David J. Weber","doi":"10.1007/s12104-022-10117-z","DOIUrl":"10.1007/s12104-022-10117-z","url":null,"abstract":"<div><p>Heterogeneous ribonuclear protein A18 (hnRNP A18) is an RNA binding protein (RBP) involved in the hypoxic cellular stress response and regulation of cytotoxic T-lymphocyte-associated protein 4 (CTLA-4) expression in melanoma, breast cancer, prostate cancer, and colon cancer solid tumors. hnRNP A18 is comprised of an N-terminal structured RNA recognition motif (RMM) and a C-terminal intrinsically disordered domain (IDD). Upon cellar stressors, such as UV and hypoxia, hnRNP A18 is phosphorylated by casein kinase 2 (CK2) and glycogen synthase kinase 3β (GSK-3β). After phosphorylation, hnRNP A18 translocates from the nucleus to the cytosol where it interacts with pro-survival mRNA transcripts for proteins such as hypoxia inducible factor 1α and CTLA-4. Both the hypoxic cellular response and modulation of immune checkpoints by cancer cells promote chemoradiation resistance and metastasis. In this study, the <sup>1</sup> H, <sup>13</sup> C, and <sup>15</sup> N backbone and sidechain resonances of the 172 amino acid hnRNP A18 were assigned sequence-specifically and provide a framework for future NMR-based drug discovery studies toward targeting hnRNP A18. These data will also enable the investigation of the dynamic structural changes within the IDD of hnRNP A18 upon phosphorylation by CK2 and GSK-3β to provide critical insight into the structure and function of IDDs.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"37 - 41"},"PeriodicalIF":0.9,"publicationDate":"2022-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-022-10117-z.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"5116317","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: 1

1H, 13C and 15N assignment of the human mitochondrial paramagnetic iron–sulfur protein CISD3 人线粒体顺磁铁硫蛋白CISD3的1H, 13C和15N分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2022-12-15 DOI: 10.1007/s12104-022-10113-3

José Malanho Silva, Deborah Grifagni, Francesca Cantini, Mario Piccioli

引用次数: 1

1H, 15N and 13C backbone resonance assignments of the acidic domain of the human MDM2 protein 人MDM2蛋白酸性结构域的1H, 15N和13C骨干共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2022-10-29 DOI: 10.1007/s12104-022-10112-4

Qinyan Song, Xiang-Qin Liu, Jan K. Rainey

{"title":"1H, 15N and 13C backbone resonance assignments of the acidic domain of the human MDM2 protein","authors":"Qinyan Song, Xiang-Qin Liu, Jan K. Rainey","doi":"10.1007/s12104-022-10112-4","DOIUrl":"10.1007/s12104-022-10112-4","url":null,"abstract":"<div><p>The human MDM2 protein regulates the tumor suppressor protein p53 by restricting its transcriptional activity and by promoting p53 degradation. MDM2 is ubiquitously expressed, with its overexpression implicated in many forms of cancer. The inhibitory effects of MDM2 on p53 have been shown to involve its N-terminal p53-binding domain and its C-terminal RING domain. The presence of an intact central acidic domain of MDM2 has also been shown to regulate p53 ubiquitination, with this domain shown to directly interact with the p53 DNA-binding domain to regulate the DNA binding activity of p53. To date, little structural information has been obtained for the MDM2 acidic domain. Thus, to gain insight into the structure and function relationship of this region, we have applied solution-state NMR spectroscopy to characterize the segment of MDM2 spanning residues 215–300. These boundaries for the acidic domain were determined on the basis of consensus observed in multiple sequence alignment. Here, we report the <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C backbone and <sup>13</sup>C<sub>β</sub> chemical shift assignments and steady-state {<sup>1</sup>H}-<sup>15</sup>N heteronuclear NOE enhancement factors as a function of residue for the acidic domain of MDM2. We show that this domain exhibits the hallmarks of being a disordered protein, on the basis both of assigned chemical shifts and residue-level backbone dynamics, with localized variation in secondary structure propensity inferred from chemical shift analysis.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"9 - 16"},"PeriodicalIF":0.9,"publicationDate":"2022-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-022-10112-4.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"5132648","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, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy 戊型肝炎病毒大结构域载脂蛋白和adp核糖结合形式的1H, 13C, 15N骨干共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2022-10-22 DOI: 10.1007/s12104-022-10111-5

Maria D. Politi, Angelo Gallo, Georgios Bouras, Maria Birkou, Bruno Canard, Bruno Coutard, Georgios A. Spyroulias

{"title":"1H, 13C, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy","authors":"Maria D. Politi, Angelo Gallo, Georgios Bouras, Maria Birkou, Bruno Canard, Bruno Coutard, Georgios A. Spyroulias","doi":"10.1007/s12104-022-10111-5","DOIUrl":"10.1007/s12104-022-10111-5","url":null,"abstract":"<div><p>The genome of Hepatitis E virus (HEV) is 7.2 kilobases long and has three open reading frames. The largest one is ORF1, encoding a non-structural protein involved in the replication process, and whose processing is ill-defined. The ORF1 protein is a multi-modular protein which includes a macro domain (MD). MDs are evolutionarily conserved structures throughout all kingdoms of life. MDs participate in the recognition and removal of ADP-ribosylation, and specifically viral MDs have been identified as erasers of ADP-ribose moieties interpreting them as important players at escaping the early stages of host-immune response. A detailed structural analysis of the <i>apo</i> and bound to ADP-ribose state of the native HEV MD would provide the structural information to understand how HEV MD is implicated in virus-host interplay and how it interacts with its intracellular partner during viral replication. In the present study we present the high yield expression of the native macro domain of HEV and its analysis by solution NMR spectroscopy. The HEV MD is folded in solution and we present a nearly complete backbone and sidechains assignment for <i>apo</i> and bound states. In addition, a secondary structure prediction by TALOS + analysis was performed. The results indicated that HEV MD has a <i>α/β/α</i> topology very similar to that of most viral macro domains.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"1 - 8"},"PeriodicalIF":0.9,"publicationDate":"2022-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-022-10111-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4880695","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