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	**[[1ni2]] – hCVIL N terminal<br />		**[[1ni2]] – hCVIL N terminal<br />
-	**[[4rm8]], [[45rm9]] – hCVIL <br />	+	**[[4rm8]], [[4rm9]] – hCVIL <br />
	**[[4rma]] – hCVIL FERM domain<br />		**[[4rma]] – hCVIL FERM domain<br />

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Revision as of 17:10, 16 October 2017

spinqualitylabelsall models Human supervillin headpiece, 2k6n Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function 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. Relevance VIL immunohisochemistry is a reliable method for diagnosing microvillus inclusion disease (MVID)[2].

3D Structures of Villin

Updated on 16-October-2017

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
2. ↑ Shillingford NM, Calicchio ML, Teot LA, Boyd T, Kurek KC, Goldsmith JD, Bousvaros A, Perez-Atayde AR, Kozakewich HP. Villin immunohistochemistry is a reliable method for diagnosing microvillus inclusion disease. Am J Surg Pathol. 2015 Feb;39(2):245-50. doi: 10.1097/PAS.0000000000000355. PMID:25517957 doi:http://dx.doi.org/10.1097/PAS.0000000000000355