View source for 2vcp


==Crystal structure of N-Wasp VC domain in complex with skeletal actin==
<StructureSection load='2vcp' size='340' side='right'caption='[[2vcp]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vcp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VCP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcp OCA], [https://pdbe.org/2vcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vcp RCSB], [https://www.ebi.ac.uk/pdbsum/2vcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vcp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/2vcp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vcp ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
Wiskott-Aldrich Syndrome Proteins (WASP) are a family of proteins that all catalyze actin filament branching with Arp2/3 complex in a variety of actin-based motile processes. The constitutively active C-terminal domain, called VCA, harbors one or more WASP Homology 2 (WH2) domains that bind G-actin, while the CA extension binds Arp2/3 complex. The VCA-actin-Arp2/3 entity associates with a mother filament to form a branched junction from which a daughter filament is initiated. The number and function of WH2-bound actin(s) in the branching process is not known, and the stoichiometry of VCA-actin-Arp2/3 complex is debated. We have expressed the tandem WH2 repeats of N-WASP, either alone (V) or associated with the C (VC) and CA (VCA) extensions. We analyze the structure of actin in complex with V, VC and VCA using protein crystallography, hydrodynamic and spectrofluorimetric methods. The partial crystal structure of VC :actin 1 :1 complex shows two actins in the asymmetric unit with extensive actin-actin contacts. In solution, each of the 2 WH2 domains in V, VC and VCA binds G-actin in 1 :2 complexes that participate in barbed end assembly. V, VC and VCA enhance barbed end depolymerization like profilin, but neither nucleate nor sever filaments, in contrast with other WH2 repeats. VCA binds Arp2/3 complex in a 1 :1 complex even in the presence of a large excess of VCA. VCA-Arp2/3 binds one actin in a Latrunculin A-sensitive fashion, in a 1 :1 :1 complex, indicating that binding of the second actin to VCA is weakened in the ternary complex.

Interactions of isolated C-terminal fragments of Neural Wiskott-Aldrich Syndrome Protein (N-WASP) with actin and Arp2/3 complex.,Gaucher JF, Mauge C, Didry D, Guichard B, Renault L, Carlier MF J Biol Chem. 2012 Jul 30. PMID:22847007<ref>PMID:22847007</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2vcp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Actin 3D structures|Actin 3D structures]]
*[[Wiskott-Aldrich syndrome protein|Wiskott-Aldrich syndrome protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Carlier MF]]
[[Category: Didry D]]
[[Category: Gaucher JF]]