Vasodilator-stimulated phosphoprotein
From Proteopedia
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==Structural highlights == | ==Structural highlights == | ||
<scene name='50/508423/Cv/9'>Human VASP complex with α-actin, profilin-1, ATP (stick model) and Ca+2 ion</scene> ([[2pbd]]). VASP binds actin with a <scene name='50/508423/Cv/10'>poly-Pro site</scene><ref>PMID:17914456</ref>. | <scene name='50/508423/Cv/9'>Human VASP complex with α-actin, profilin-1, ATP (stick model) and Ca+2 ion</scene> ([[2pbd]]). VASP binds actin with a <scene name='50/508423/Cv/10'>poly-Pro site</scene><ref>PMID:17914456</ref>. | ||
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</StructureSection> | </StructureSection> | ||
==3D structure of vasodilator-stimulated phosphoprotein== | ==3D structure of vasodilator-stimulated phosphoprotein== | ||
Revision as of 14:43, 14 January 2021
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3D structure of vasodilator-stimulated phosphoprotein
Updated on 14-January-2021
1egx – hVASP EVH1 domain – human – NMR
1usd, 1use - hVASP tetramerization domain
2pav, 2pbd, 3chw – hVASP + actin + profilin-1
2v8c – hVASP + profilin-2
References
- ↑ Wentworth JK, Pula G, Poole AW. Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets. Biochem J. 2006 Jan 15;393(Pt 2):555-64. PMID:16197368 doi:http://dx.doi.org/BJ20050796
- ↑ Lee SY, Gertler FB, Goldberg MB. Vasodilator-stimulated phosphoprotein restricts cell-to-cell spread of Shigella flexneri at the cell periphery. Microbiology. 2015 Nov;161(11):2149-60. doi: 10.1099/mic.0.000173. Epub 2015 Sep , 9. PMID:26358985 doi:http://dx.doi.org/10.1099/mic.0.000173
- ↑ Ferron F, Rebowski G, Lee SH, Dominguez R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 2007 Oct 31;26(21):4597-606. Epub 2007 Oct 4. PMID:17914456

