Villin

From Proteopedia
Revision as of 09:34, 21 August 2014 by Michal Harel (talk | contribs)
Jump to navigationJump to search

Template:STRUCTURE 2k6n

  • 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.

3D Structures of Villin

Updated on 21-August-2014

Supervillin

2k6m, 2k6n – hSVIL headpiece– human – NMR

Villin

3fg7 – hVIL gelsolin domains 4-6
2llf - hVIL gelsolin-like domain 6 - NMR
1unc – hVIL headpiece
3iur - hVIL headpiece H2H3 helices+prolyl endopeptidase – Aeromonas punctata
2rjw, 2rjx, 2rjv, 2rjy, 1yu7, 1yu8 – cVIL headpiece (mutant) – chicken
1yu5, 1qqv - cVIL headpiece
3myc, 3mye, 3nkj, 3mya, 3tjw, 3trv, 3trw, 3try - cVIL headpiece (mutant)
1vii, 2vik, 2vil - cVIL headpiece - NMR
2ppz, 2jm0 - VIL headpiece (mutant) – synthetic – NMR
2f4k, 1wy3, 1wy4, 1yrf, 1yri - VIL fragment (mutant) – synthetic

Advillin

1und – hAVIL headpiece

Cytovillin

1ni2 – hCVIL N terminal


References

  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