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Vasodilator-stimulated phosphoprotein

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Human VASP (dark olive) complex with α-actin (cyan), profilin-1 (green), ATP (stick model) and Ca+2 ion (green), 2pbd

Drag the structure with the mouse to rotate

3D structure of vasodilator-stimulated phosphoprotein

Updated on 17-March-2024

1egx – hVASP EVH1 domain – human – NMR
1usd, 1use - hVASP tetramerization domain
2pav, 2pbd, 3chw – hVASP + actin + profilin-1
2v8c – hVASP + profilin-2
8gat, 8gau – hVASP/neuroaminidase + antibody – Cryo EM

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

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