Vasodilator-stimulated phosphoprotein: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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-== Your Heading Here (maybe something like 'Structure') ==
+<StructureSection load='' size='350' side='right' caption='Human VASP (dark olive) complex with α-actin (cyan), profilin-1 (green), ATP (stick model) and Ca+2 ion (green), [[2pbd]]' scene='50/508423/Cv/7' >
-<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
+== Function ==
-Anything in this section will appear adjacent to the 3D structure and will be scrollable.
+'''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<ref>PMID:16197368</ref>.  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]].
-</StructureSection>
+== Relevance ==
+VASP restricts the spread of Shigella  which causes diarrhoreal disease<ref>PMID:26358985</ref>.
-'''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.
+==Structural highlights ==
-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.
+<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>.
-For more details see [[Group:MUZIC:Mena_VASP]].
+</StructureSection>
 ==3D structure of vasodilator-stimulated phosphoprotein==
-[[1egx]] – hVASP EVH1 domain – human – NMR<BR />
+Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-[[1usd]], [[1use]] - hVASP tetramerization domain<br />
-[[2pav]], [[2pbd]], [[3chw]] – hVASP + actin + profilin-1
+[[1egx]] – hVASP EVH1 domain 1-115 – human – NMR<BR />
+[[1use]] - hVASP tetramerization domain 335-379<br />
+[[1usd]] - hVASP tetramerization domain (mutant)<br />
+[[2pav]], [[3chw]] – hVASP 199-214 + actin + profilin-1<br />
+[[2pbd]] – hVASP poly Pro domain 203-245 + actin + profilin-1<br />
+[[2v8c]] – hVASP 165-184 + profilin-2<br />
+[[8gat]], [[8gau]] – hVASP tetramerization domain/neuroaminidase + antibody – Cryo EM<BR />
+==References==
+<references />
+[[Category:Topic Page]]