Villin

From Proteopedia

proteopedia linkproteopedia link

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. images on the left and right correspond to one representative villin structure, i.e. the human supervillin headpiece (2k6n).

3D Structures of Villin

Updated on 24-November-2013

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