دورية أكاديمية
أعرض في EDS

Capturing conformational States in proteins using sparse paramagnetic NMR data.

التفاصيل البيبلوغرافية
العنوان: Capturing conformational States in proteins using sparse paramagnetic NMR data.
المؤلفون: Pilla KB; Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia., Leman JK; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, 21218, United States of America., Otting G; Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia., Huber T; Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.
المصدر: PloS one [PLoS One] 2015 May 18; Vol. 10 (5), pp. e0127053. Date of Electronic Publication: 2015 May 18 (Print Publication: 2015).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Nuclear Magnetic Resonance, Biomolecular* , Protein Conformation*, Proteins/*chemistry, Amino Acid Sequence ; Models, Molecular ; Protein Binding ; Proteins/metabolism ; Serine Endopeptidases/chemistry ; Serine Endopeptidases/metabolism ; Solutions ; Structure-Activity Relationship ; Viral Nonstructural Proteins/chemistry
مستخلص: Capturing conformational changes in proteins or protein-protein complexes is a challenge for both experimentalists and computational biologists. Solution nuclear magnetic resonance (NMR) is unique in that it permits structural studies of proteins under greatly varying conditions, and thus allows us to monitor induced structural changes. Paramagnetic effects are increasingly used to study protein structures as they give ready access to rich structural information of orientation and long-range distance restraints from the NMR signals of backbone amides, and reliable methods have become available to tag proteins with paramagnetic metal ions site-specifically and at multiple sites. In this study, we show how sparse pseudocontact shift (PCS) data can be used to computationally model conformational states in a protein system, by first identifying core structural elements that are not affected by the environmental change, and then computationally completing the remaining structure based on experimental restraints from PCS. The approach is demonstrated on a 27 kDa two-domain NS2B-NS3 protease system of the dengue virus serotype 2, for which distinct closed and open conformational states have been observed in crystal structures. By changing the input PCS data, the observed conformational states in the dengue virus protease are reproduced without modifying the computational procedure. This data driven Rosetta protocol enables identification of conformational states of a protein system, which are otherwise difficult to obtain either experimentally or computationally.
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المشرفين على المادة: 0 (Proteins)
0 (Solutions)
0 (Viral Nonstructural Proteins)
EC 3.4.21.- (NS3 protease, dengue virus)
EC 3.4.21.- (Serine Endopeptidases)
تواريخ الأحداث: Date Created: 20150521 Date Completed: 20160406 Latest Revision: 20181113
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC4436263
DOI: 10.1371/journal.pone.0127053
PMID: 25992808
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0127053