Vasodilator-stimulated phosphoprotein: Difference between revisions
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{{STRUCTURE_2pbd| PDB=2pbd | SIZE=400| SCENE= |right|CAPTION=Human VASP complex with actin, profilin-1, ATP and Ca+2 ion, [[2pbd]] }} | {{STRUCTURE_2pbd| PDB=2pbd | SIZE=400| SCENE= |right|CAPTION=Human VASP (dark olive) complex with α-actin (grey), profilin-1 (green), ATP and Ca+2 ion (green), [[2pbd]] }} | ||
'''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 associated with filament formation and promotes elongation. | '''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 associated with filament formation and promotes elongation. | ||
Revision as of 17:21, 18 November 2012
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 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.
3D structure of vasodilator-stimulated phosphoprotein3D structure of vasodilator-stimulated phosphoprotein
1egx – hVASP EVH1 domain – human – NMR
1usd, 1use - hVASP tetramerization domain
2pav, 2pbd, 3chw – hVASP + actin + profilin-1