Biomolecular NMR Assignments最新文献_第5页

1H, 15N and13C resonance assignments of S2A mutant of human carbonic anhydrase II 人碳酸酐酶 II S2A 突变体的 1H、15N 和 13C 共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-03-23 DOI: 10.1007/s12104-024-10166-6

Neelam, Himanshu Singh

引用次数: 0

Backbone 1H, 13C and 15N resonance assignment of the ubiquitin specific protease 7 catalytic domain (residues 208–554) in complex with a small molecule ligand 泛素特异性蛋白酶 7 催化结构域（残基 208-554）与小分子配体复合物的骨架 1H、13C 和 15N 共振赋值。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-03-12 DOI: 10.1007/s12104-024-10165-7

Maya J. Pandya, Wojciech Augustyniak, Matthew J. Cliff, Ilka Lindner, Anne Stinn, Jan Kahmann, Koen Temmerman, Hugh R. W. Dannatt, Jonathan P. Waltho, Martin J. Watson

引用次数: 0

Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2 人类 SERF2 的骨架 1H、13C 和 15N 化学位移分布图

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-03-11 DOI: 10.1007/s12104-024-10167-5

Bikash R. Sahoo, Vivekanandan Subramanian, James C.A. Bardwell

{"title":"Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2","authors":"Bikash R. Sahoo, Vivekanandan Subramanian, James C.A. Bardwell","doi":"10.1007/s12104-024-10167-5","DOIUrl":"10.1007/s12104-024-10167-5","url":null,"abstract":"<div>Human small EDRK-rich factor protein SERF2 is a cellular driver of protein amyloid formation, a process that has been linked to neurodegenerative diseases including Alzheimer’s and Parkinson’s disease. SERF2 is a 59 amino acid protein, highly charged, and well conserved whose structure and physiological function is unclear. SERF family proteins including human SERF2 have shown a tendency to form fuzzy complexes with misfolded proteins such as α-Synuclein which has been linked to Parkinson’s disease. SERF family proteins have been recently identified to bind nucleic acids, but the binding mechanism(s) remain enigmatic. Here, using multidimensional solution NMR, we report the 1H, 15N, and 13C chemical shift assignments (~ 86% of backbone resonance assignments) for human SERF2. TALOS-N predicted secondary structure of SERF2 showed three very short helices (3–4 residues long) in the N-terminal region of the protein and a long helix in the C-terminal region spanning residues 37–46 which is consistent with the helical content indicated by circular dichroism spectroscopy. Paramagnetic relaxation enhancement NMR analysis revealed that a short C-terminal region E53-K55 is in the proximity of the N-terminus. Having the backbone assignment of SERF2 allowed us to probe its interaction with α-Synuclein and to identify the residues in SERF2 binding interfaces that likely promote α-Synuclein aggregation.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 1","pages":"51 - 57"},"PeriodicalIF":0.8,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140099982","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

NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4 来自动点核蛋白 KKT4 的 BRCT 结构域的核磁共振研究。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-03-07 DOI: 10.1007/s12104-024-10163-9

Patryk Ludzia, Hanako Hayashi, Timothy Robinson, Bungo Akiyoshi, Christina Redfield

{"title":"NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4","authors":"Patryk Ludzia, Hanako Hayashi, Timothy Robinson, Bungo Akiyoshi, Christina Redfield","doi":"10.1007/s12104-024-10163-9","DOIUrl":"10.1007/s12104-024-10163-9","url":null,"abstract":"<div>KKT4 is a multi-domain kinetochore protein specific to kinetoplastids, such as Trypanosoma brucei. It lacks significant sequence similarity to known kinetochore proteins in other eukaryotes. Our recent X-ray structure of the C-terminal region of KKT4 shows that it has a tandem BRCT (BRCA1 C Terminus) domain fold with a sulfate ion bound in a typical binding site for a phosphorylated serine or threonine. Here we present the 1H, 13C and 15N resonance assignments for the BRCT domain of KKT4 (KKT4463–645) from T. brucei. We show that the BRCT domain can bind phosphate ions in solution using residues involved in sulfate ion binding in the X-ray structure. We have used these assignments to characterise the secondary structure and backbone dynamics of the BRCT domain in solution. Mutating the residues involved in phosphate ion binding in T. brucei KKT4 BRCT results in growth defects confirming the importance of the BRCT phosphopeptide-binding activity in vivo. These results may facilitate rational drug design efforts in the future to combat diseases caused by kinetoplastid parasites.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 1","pages":"15 - 25"},"PeriodicalIF":0.8,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11081923/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140058298","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 resonance assignments of hepatocyte nuclear factor-1-beta (HNF1β) POUS and POUHD 肝细胞核因子-1-β（HNF1β）POUS 和 POUHD 的 1H、13C 和 15N 主干共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-03-07 DOI: 10.1007/s12104-024-10168-4

Sayaka Hokazono, Eri Imagawa, Daishi Hirano, Takahisa Ikegami, Kimihiko Oishi, Tsuyoshi Konuma

{"title":"1H, 13C and 15N backbone resonance assignments of hepatocyte nuclear factor-1-beta (HNF1β) POUS and POUHD","authors":"Sayaka Hokazono, Eri Imagawa, Daishi Hirano, Takahisa Ikegami, Kimihiko Oishi, Tsuyoshi Konuma","doi":"10.1007/s12104-024-10168-4","DOIUrl":"10.1007/s12104-024-10168-4","url":null,"abstract":"<div>Hepatocyte nuclear factor 1β (HNF1β) is a transcription factor that plays a key role in the development and function of the liver, pancreas, and kidney. HNF1β plays a key role in early vertebrate development and the morphogenesis of these organs. In humans, heterozygous mutations in the HNF1B gene can result in organ dysplasia, making it the most common cause of developmental renal diseases, including renal cysts, renal malformations, and familial hypoplastic glomerular cystic kidney disease. Pathogenic variants in the HNF1B gene are known to cause various diseases, including maturity-onset diabetes of the young and developmental renal diseases. This study presents the backbone resonance assignments of HNF1β POUS and POUHD domains, which are highly conserved domains required for the recognition of double-stranded DNA. Our data will be useful for NMR studies to verify the altered structures and functions of mutant HNF1B proteins that can induce developmental renal diseases, including renal cysts, renal malformations, and familial hypoplastic glomerular cystic kidney disease. This study will provide the structural basis for future studies to elucidate the molecular mechanisms underlying how mutations in HNF1β cause diseases.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 1","pages":"59 - 63"},"PeriodicalIF":0.8,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140048452","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 the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana 拟南芥介导复合体亚基 MED25 的 ACID 结构域的化学位移分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-02-09 DOI: 10.1007/s12104-024-10164-8

Yue Xiong, Jiang Zhu, Rui Hu, Ying Li, Yunhuang Yang, Maili Liu

引用次数: 0

NMR 1H, 13C, 15N backbone resonance assignments of wild-type human K-Ras and its oncogenic mutants G12D and G12C bound to GTP 野生型人K-Ras及其与GTP结合的致癌突变体G12D和G12C的NMR 1H、13C、15N骨架共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-11-10 DOI: 10.1007/s12104-023-10162-2

Chunhua Yuan, Alexandar L. Hansen, Lei Bruschweiler-Li, Rafael Brüschweiler

引用次数: 0

13C and 15N resonance assignments of alpha synuclein fibrils amplified from Lewy Body Dementia tissue Lewy体痴呆组织中α-突触核蛋白原纤维的13C和15N共振定位

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-11-03 DOI: 10.1007/s12104-023-10156-0

Alexander M. Barclay, Dhruva D. Dhavale, Collin G. Borcik, Moses H. Milchberg, Paul T. Kotzbauer, Chad M. Rienstra

引用次数: 0

Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM 金黄色葡萄球菌LytM催化结构域的化学位移分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-11-02 DOI: 10.1007/s12104-023-10161-3

Helena Tossavainen, Ilona Pitkänen, Lina Antenucci, Chandan Thapa, Perttu Permi

{"title":"Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM","authors":"Helena Tossavainen, Ilona Pitkänen, Lina Antenucci, Chandan Thapa, Perttu Permi","doi":"10.1007/s12104-023-10161-3","DOIUrl":"10.1007/s12104-023-10161-3","url":null,"abstract":"<div>S. aureus resistance to antibiotics has increased rapidly. MRSA strains can simultaneously be resistant to many different classes of antibiotics, including the so-called “last-resort” drugs. Resistance complicates treatment, increases mortality and substantially increases the cost of treatment. The need for new drugs against (multi)resistant S. aureus is high. M23B family peptidoglycan hydrolases, enzymes that can kill S. aureus by cleaving glycine-glycine peptide bonds in S. aureus cell wall are attractive targets for drug development because of their binding specificity and lytic activity. M23B enzymes lysostaphin, LytU and LytM have closely similar catalytic domain structures. They however differ in their lytic activities, which can arise from non-conserved residues in the catalytic groove and surrounding loops or differences in dynamics. We report here the near complete 1H/13C/15N resonance assignment of the catalytic domain of LytM, residues 185–316. The chemical shift data allow comparative structural and functional studies between the enzymes and is essential for understanding how these hydrolases degrade the cell wall.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 1","pages":"1 - 5"},"PeriodicalIF":0.8,"publicationDate":"2023-11-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11082022/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71419439","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

Correction to: NMR resonance assignments of 18.5 kDa complex of Arabidopsis thaliana DRB7.2:DRB4 interaction domains 更正：拟南芥DRB7.2的18.5kDa复合物的NMR共振分配：DRB4相互作用结构域。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-11-01 DOI: 10.1007/s12104-023-10152-4

Sneha Paturi, Mandar V. Deshmukh

引用次数: 0