Vasodilator-stimulated phosphoprotein

spinqualitylabelsall models Human VASP (dark olive) complex withα-actin (cyan), profilin-1 (green), ATP (stick model) and Ca+2 ion (green), 2pbd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Vasodilator-stimulated phosphoprotein (VASP) belongs to the Ena-VASP family. It binds proteins with E/DFPPPPXD/E motif and targets them to focal adhesion cell membranes. VASP is an actin- and profilin-binding protein. VASP is associated with filament formation and promotes elongation. VASP protects the actin barb edge against capping and increases the rate of actin polymerization in the presence of capping protein. VASP is a homotetramer. For more details see Group:MUZIC:Mena_VASP. Relevance VASP restricts the spread of Shigella which causes diarrhoreal disease. Structural highlights Human VASP complex with α-actin, profilin-1, ATP (stick model) and Ca+2 ion (2pbd). VASP binds actin with a poly-Pro site.

3D structure of vasodilator-stimulated phosphoprotein

Updated on 22-August-2024

1egx – hVASP EVH1 domain 1-115 – human – NMR
2pbd - hVASP tetramerization domain 335-379
1usd - hVASP tetramerization domain (mutant)
2pav, 3chw – hVASP 199-214 + actin + profilin-1
2pbd – hVASP poly Pro domain 203-245 + actin + profilin-1
2v8c – hVASP 165-184 + profilin-2
8gat, 8gau – hVASP tetramerization domain/neuroaminidase + antibody – Cryo EM

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman