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| [[Image:Tr.png|left|200px|thumb|Crystal structure of human full-length Vinculin, [[1tr2]]]]
| | <StructureSection load='1st6' size='340' side='right' caption='Chicken full-length metavinculin, [[1st6]]' scene='' > |
| {{STRUCTURE_1tr2| PDB=1tr2 | SIZE=300| SCENE=Vinculin/Cv/2 |right|CAPTION=Human full-length Vinculin, [[1tr2]] }}
| | == Function == |
| | [[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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| [[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. 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]]). <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.
| | == Relevance == |
| | 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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| | == Disease == |
| | Mutation in m-VCL can yield cardiomyopathic phenotype<ref>PMID:16236538</ref>. |
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| | == Structural highlights == |
| | <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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| == 3D Structures of Vinculin == | | == 3D Structures of Vinculin == |
| | [[Vinculin 3D structures]] |
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| ''Update July 2012''
| | ==References== |
| | | <references /> |
| | | </StructureSection> |
| [[3h2u]] – hVCL Vd1 + raver1 RRM - human<br />
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| [[3h2v]] - hVCL C-terminal + raver1 RRM<br />
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| [[2ibf]], [[2hsq]], [[2gww]] - hVCL Vd1 + SfVCL binding sites from ''Shigella flexneri''<br />
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| [[1tr2]] – hVCL<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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| [[1qkr]] – hVCL C-terminal<br />
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| ==Metavinculin== | |
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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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| [[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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| [[Category:Topic Page]] | | [[Category:Topic Page]] |
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| Created with the participation of [[User:Susan Craig|Susan Craig]]. | | *Created with the participation of [[User:Susan Craig|Susan Craig]]. |