Vinculin

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<StructureSection load='1st6' size='340' side='right' caption='Chicken full-length metavinculin, [[1st6]]' scene='' >
<StructureSection load='1st6' size='340' side='right' caption='Chicken full-length metavinculin, [[1st6]]' scene='' >
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[[Vinculin|Vinculins]] (VCLs) are involved in adhesion by linking integrin molecules to the actin cytoskeleton. Its head domain (Vd1) can bind to [[Talin|talin]] or to [[Actinin|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. <scene name='Sandbox_27/Role_i997_vinculin_head-tail_1/1'>Vinculin Autoinhibition</scene> 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.
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== Function ==
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</StructureSection>
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[[Vinculin|Vinculins]] (VCLs) are involved in adhesion by linking integrin molecules to the actin cytoskeleton. Its head domain (Vd1) can bind to [[Talin|talin]] or to [[Actinin|alpha-actinin]] at their respective VCL Binding Sites (VBS)<ref>PMID:11152287</ref>. The protein raver1 RNA Recognition Motif (RRM) forms a complex with VCL or m-VCL. '''Metavinculin''' (m-VCL) is a splice version of VCL containing an extra ca. 70 amino acids in the C-terminal domain.
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== 3D Structures of Vinculin ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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== Relevance ==
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{{#tree:id=OrganizedByTopic|openlevels=0|
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Loss of VCL could be used as a prognostic factor for colorectal cancer se it promotes metastasis<ref>PMID:25496021</ref>.
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*Vinculin
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== Disease ==
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Mutation in m-VCL can yield cardiomyopathic phenotype<ref>PMID:16236538</ref>.
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**[[1tr2]] – hVCL - human<br />
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== Structural highlights ==
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**[[1qkr]] – hVCL C-terminal<br />
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<scene name='Sandbox_27/Role_i997_vinculin_head-tail_1/1'>Vinculin Autoinhibition</scene> is achieved through a high affinity intramolecular interaction between tail (orange) and head (aqua) domains ([[1st6]]). Energetically, I997 is key to maintaining this autoinhibition.
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**[[3h2v]] - hVCL C-terminal + raver1 RRM<br />
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**[[4pr9]] - hVCL C-terminal + lipid<br />
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**[[3h2u]] – hVCL Vd1 + raver1 RRM <br />
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**[[2ibf]], [[2hsq]], [[2gww]] - hVCL Vd1 + SfVCL binding sites from ''Shigella flexneri''<br />
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**[[1ydi]] - hVCL Vd1+hActinin VBS<br />
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**[[1t01]] - cVCL Vd1+mTalin VBS – chicken<br />
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**[[1syq]], [[1rkc]], [[1rke]] – hVCL Vd1+hTalin VBS<br />
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**[[3zdl]] – cVCL Vd1 + amyloid β precursor protein N terminal<br />
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*Metavinculin
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== 3D Structures of Vinculin ==
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[[Vinculin 3D structures]]
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**[[3myi]] – m-VCL tail domain <br />
 
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**[[3rf3]] - hm-VCL + invasin IPAA<br />
 
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**[[3s90]] - hm-VCL head domain + mTalin-1 peptide<br />
 
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**[[4dj9]] - hm-VCL head domain + hTalin-1 peptide <br />
 
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**[[3tj5]] - hm-VCL head domain + Sca-family protein peptide<br />
 
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**[[3tj6]] - hm-VCL head domain + protein Ps 120 peptide<br />
 
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**[[4ehp]] - hm-VCL head domain + catenin α-1 residues 277-382<br />
 
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**[[3vf0]] – hm-VCL residues 856-1134 + ribonucleoprotein PTB-binding<br />
 
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**[[2gdc]] – cm-VCL Vd1+SfInvasin C-terminal <br />
 
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**[[1xwj]] - cm-VCL Vd1+cTalin VBS3<br />
 
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**[[1zvz]], [[1zw2]], [[1zw3]], [[1u6h]] - cm-VCL Vd1+cTalin rod<br />
 
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**[[1st6]] – cm-VCL<br />
 
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**[[4e17]], [[4e18]] - cm-VCL Vd1 + catenin α-1 VCL-binding domain
 
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}}
 
==References==
==References==
<references />
<references />
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</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]
*Created with the participation of [[User:Susan Craig|Susan Craig]].
*Created with the participation of [[User:Susan Craig|Susan Craig]].

Current revision

Chicken full-length metavinculin, 1st6

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky

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