Villin: Difference between revisions

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{{STRUCTURE_2k6n| right| PDB=2k6n  |  SCENE=Villin/Cv/1 |CAPTION=Human supervillin headpiece, [[2k6n]] }}
 
<StructureSection load='2k6n' size='340' side='right' caption='Human supervillin headpiece, [[2k6n]]' scene='Villin/Cv/1' >
<StructureSection load='2k6n' size='340' side='right' caption='Human supervillin headpiece, [[2k6n]]' scene='Villin/Cv/1' >
* [[Villin]] (VIL) is an actin-binding protein.  It contains gelsolin-like domains in its N-terminal and a helical headpiece which binds actin<ref>PMID:10480879</ref>.<br />
* [[Villin]] (VIL) is an actin-binding protein.  It contains gelsolin-like domains in its N-terminal and a helical headpiece which binds actin<ref>PMID:10480879</ref>.<br />

Revision as of 11:51, 13 December 2016

  • Villin (VIL) is an actin-binding protein. It contains gelsolin-like domains in its N-terminal and a helical headpiece which binds actin[1].
  • Supervillin (SVIL) contains numerous gelsolin-like domains in its C-terminal and interacts with actin.
  • Advillin (AVIL) is another actin-binding protein in the gelsolin superfamily which is expressed in the peripheral sensory neurons.
  • Cytovillin (CVIL) or ezrin or villin-2 serves as intermediate between plasma membrane and actin cytoskeleton.

Human supervillin headpiece, 2k6n

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3D Structures of Villin3D Structures of Villin

Updated on 13-December-2016

ReferencesReferences

  1. Friederich E, Vancompernolle K, Louvard D, Vandekerckhove J. Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro. J Biol Chem. 1999 Sep 17;274(38):26751-60. PMID:10480879

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Alexander Berchansky, Michal Harel, David Canner, Jaime Prilusky, Joel L. Sussman