Vasodilator-stimulated phosphoprotein
From Proteopedia
(Difference between revisions)
(New page: == Your Heading Here (maybe something like 'Structure') == <StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry 1dq8)' scene=''> Any...) |
|||
| Line 1: | Line 1: | ||
| - | == | + | {{STRUCTURE_2pbd| PDB=2pbd | SIZE=400| SCENE= |right|CAPTION=Human VASP complex with actin and profilin-1, [[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 09:57, 5 August 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 phosphoprotein
1egx – hVASP EVH1 domain – human – NMR
1usd, 1use - hVASP tetramerization domain
2pav, 2pbd, 3chw – hVASP + actin + profilin-1
