About: NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein     Goto   Sponge   NotDistinct   Permalink

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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 has been 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 the traditional 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 the WASp-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 assignment.
  • 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 has been 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 the traditional 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 the WASp-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 assignment. (en)
Title
  • NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein
  • NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein (en)
skos:prefLabel
  • NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein
  • NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein (en)
skos:notation
  • RIV/00216224:14740/13:00066376!RIV14-GA0-14740___
http://linked.open...avai/riv/aktivita
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  • P(GAP206/11/0758)
http://linked.open...iv/cisloPeriodika
  • 2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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  • 91849
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  • RIV/00216224:14740/13:00066376
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  • WISKOTT-ALDRICH-SYNDROME; NUCLEAR-MAGNETIC-RESONANCE; SEQUENCE-SPECIFIC ASSIGNMENT; PROLINE-RICH REGIONS; 8 M UREA; CHEMICAL-SHIFTS; ALPHA-SYNUCLEIN; N-WASP; ACTIN POLYMERIZATION; POLYPROLINE-II (en)
http://linked.open.../riv/klicoveSlovo
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  • US - Spojené státy americké
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  • [8521938259A0]
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  • Biophysical Journal
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http://linked.open...ichTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...v/svazekPeriodika
  • 105
http://linked.open...iv/tvurceVysledku
  • Nováček, Jiří
  • Žídek, Lukáš
  • Chill, Jordan H
  • Haba, Noam Y
  • Barda-Saad, Mira
  • Gross, Renana
  • Shaked, Hadassa
http://linked.open...ain/vavai/riv/wos
  • 000321941700021
issn
  • 0006-3495
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.bpj.2013.05.046
http://localhost/t...ganizacniJednotka
  • 14740
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