NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F13%3A00066376" target="_blank" >RIV/00216224:14740/13:00066376 - isvavai.cz</a>

Result on the web

<a href="http://www.ncbi.nlm.nih.gov/pubmed/23870269" target="_blank" >http://www.ncbi.nlm.nih.gov/pubmed/23870269</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpj.2013.05.046" target="_blank" >10.1016/j.bpj.2013.05.046</a>

Result language

angličtina

Original language name

NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein

Original language description

WASp-interacting protein (WIP) is a 503-residue proline-rich polypeptide expressed in human T cells. The WIP C-terminal domain binds to Wiskott-Aldrich syndrome protein (WASp) and regulates its activation and degradation, and the WIP-WASp interaction hasbeen shown to be critical for actin polymerization and implicated in the onset of WAS and X-linked thrombocytopenia. WIP is predicted to be an intrinsically disordered protein, a class of polypeptides that are of great interest because they violate thetraditional structure-function paradigm. In this first (to our knowledge) study of WIP in its unbound state, we used NMR to investigate the biophysical behavior of WIPC, a C-terminal domain fragment of WIP that includes residues 407-503 and contains theWASp-binding site. In light of the poor spectral dispersion exhibited by WIPC and the high occurrence (25%) of proline residues, we employed 5D-(NMRC)-C-13-detected NMR experiments with nonuniform sampling to accomplish full resonance ass

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/GAP206%2F11%2F0758" target="_blank" >GAP206/11/0758: Development of high-resolution methodology for NMR studies of disordered proteins with highly degenerated resonance frequencies</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2013

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biophysical Journal

ISSN

0006-3495

e-ISSN

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Volume of the periodical

105

Issue of the periodical within the volume

2

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

481-493

UT code for WoS article

000321941700021

EID of the result in the Scopus database

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