Vinculin: Difference between revisions

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*Vinculin
*Vinculin


**[[3h2u]] – hVCL Vd1 + raver1 RRM - human<br />
**[[1tr2]] – hVCL - human<br />
**[[1qkr]] – hVCL C-terminal<br />
**[[3h2v]] - hVCL C-terminal + raver1 RRM<br />
**[[3h2v]] - hVCL C-terminal + raver1 RRM<br />
**[[4pr9]] - hVCL C-terminal + lipid<br />
**[[3h2u]] – hVCL Vd1 + raver1 RRM <br />
**[[2ibf]], [[2hsq]], [[2gww]] - hVCL Vd1 + SfVCL binding sites from ''Shigella flexneri''<br />
**[[2ibf]], [[2hsq]], [[2gww]] - hVCL Vd1 + SfVCL binding sites from ''Shigella flexneri''<br />
**[[1tr2]] – hVCL<br />
**[[1ydi]] - hVCL Vd1+hActinin VBS<br />
**[[1ydi]] - hVCL Vd1+hActinin VBS<br />
**[[1t01]] - cVCL Vd1+mTalin VBS – chicken<br />
**[[1t01]] - cVCL Vd1+mTalin VBS – chicken<br />
**[[1syq]], [[1rkc]], [[1rke]] – hVCL Vd1+hTalin VBS<br />
**[[1syq]], [[1rkc]], [[1rke]] – hVCL Vd1+hTalin VBS<br />
**[[1qkr]] – hVCL C-terminal<br />
**[[3zdl]] – cVCL Vd1 + amyloid β precursor protein N terminal<br />
**[[3zdl]] – cVCL Vd1 + amyloid β precursor protein N terminal<br />



Revision as of 11:19, 25 June 2015

Template:STRUCTURE 1st6

Vinculins (VCLs) are involved in adhesion by linking integrin molecules to the actin cytoskeleton. Its head domain (Vd1) can bind to talin or to alpha-actinin at their respective VCL Binding Sites (VBS). A splice variant of vinculin is meta-vinculin (m-VCL). The protein raver1 RNA Recognition Motif (RRM) forms a complex with VCL or m-VCL. The images at the left and at the right correspond to one representative Vinculin structure, i.e. crystal structure of human full-length Vinculin (1tr2). is achieved through a high affinity intramolecular interaction between tail (orange) and head (aqua) domains (1st6). Energetically, I997 is key to maintaining this autoinhibition. Metavinculin is a splice version of VCL containing an extra ca. 70 amino acids in the C-terminal domain.

3D Structures of Vinculin3D Structures of Vinculin

Updated on 25-June-2015

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky, Michal Harel