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rdf:type
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rdfs:seeAlso
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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)
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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)
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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)
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skos:notation
| - RIV/00216224:14740/13:00066376!RIV14-GA0-14740___
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14740/13:00066376
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - 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)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Nováček, Jiří
- Žídek, Lukáš
- Chill, Jordan H
- Haba, Noam Y
- Barda-Saad, Mira
- Gross, Renana
- Shaked, Hadassa
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http://linked.open...ain/vavai/riv/wos
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issn
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number of pages
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http://bibframe.org/vocab/doi
| - 10.1016/j.bpj.2013.05.046
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http://localhost/t...ganizacniJednotka
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