1egx: Difference between revisions

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[[Image:1egx.png|left|200px]]


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==SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)==
The line below this paragraph, containing "STRUCTURE_1egx", creates the "Structure Box" on the page.
<StructureSection load='1egx' size='340' side='right'caption='[[1egx]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1egx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1egx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egx OCA], [https://pdbe.org/1egx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egx RCSB], [https://www.ebi.ac.uk/pdbsum/1egx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egx ProSAT]</span></td></tr>
{{STRUCTURE_1egx|  PDB=1egx  |  SCENE=  }}
</table>
 
== Function ==
===SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)===
[https://www.uniprot.org/uniprot/VASP_HUMAN VASP_HUMAN] Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.<ref>PMID:7828592</ref> <ref>PMID:10087267</ref> <ref>PMID:10438535</ref> <ref>PMID:15939738</ref> <ref>PMID:17082196</ref> <ref>PMID:18559661</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egx_consurf.spt"</scriptWhenChecked>
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==About this Structure==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1egx ConSurf].
[[1egx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGX OCA].  
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Group:MUZIC:Mena VASP|MUZIC:Mena VASP]]
*[[Vasodilator-stimulated phosphoprotein|Vasodilator-stimulated phosphoprotein]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:010990454</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ball, L.]]
[[Category: Large Structures]]
[[Category: Hafner, A.]]
[[Category: Ball L]]
[[Category: Hof, M.]]
[[Category: Hafner A]]
[[Category: Hoffmann, B.]]
[[Category: Hof M]]
[[Category: Jarchau, T.]]
[[Category: Hoffmann B]]
[[Category: Kuhne, R.]]
[[Category: Jarchau T]]
[[Category: Oschkinat, H.]]
[[Category: Kuhne R]]
[[Category: Schmieder, P.]]
[[Category: Oschkinat H]]
[[Category: Schneider-Mergener, J.]]
[[Category: Schmieder P]]
[[Category: Volkmer-Engert, R.]]
[[Category: Schneider-Mergener J]]
[[Category: Wahl, M.]]
[[Category: Volkmer-Engert R]]
[[Category: Walter, U.]]
[[Category: Wahl M]]
[[Category: Evh1]]
[[Category: Walter U]]
[[Category: Poly-proline-binding domain]]
[[Category: Z-disk]]
[[Category: Signaling protein]]
[[Category: Vasp-ena]]

Latest revision as of 13:02, 20 March 2024

SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)

Structural highlights

1egx is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VASP_HUMAN Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Haffner C, Jarchau T, Reinhard M, Hoppe J, Lohmann SM, Walter U. Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. EMBO J. 1995 Jan 3;14(1):19-27. PMID:7828592
  2. ↑ Laurent V, Loisel TP, Harbeck B, Wehman A, Grobe L, Jockusch BM, Wehland J, Gertler FB, Carlier MF. Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J Cell Biol. 1999 Mar 22;144(6):1245-58. PMID:10087267
  3. ↑ Bachmann C, Fischer L, Walter U, Reinhard M. The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. J Biol Chem. 1999 Aug 13;274(33):23549-57. PMID:10438535
  4. ↑ Barzik M, Kotova TI, Higgs HN, Hazelwood L, Hanein D, Gertler FB, Schafer DA. Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins. J Biol Chem. 2005 Aug 5;280(31):28653-62. Epub 2005 Jun 6. PMID:15939738 doi:10.1074/jbc.M503957200
  5. ↑ Blume C, Benz PM, Walter U, Ha J, Kemp BE, Renne T. AMP-activated protein kinase impairs endothelial actin cytoskeleton assembly by phosphorylating vasodilator-stimulated phosphoprotein. J Biol Chem. 2007 Feb 16;282(7):4601-12. Epub 2006 Nov 2. PMID:17082196 doi:10.1074/jbc.M608866200
  6. ↑ Li Calzi S, Purich DL, Chang KH, Afzal A, Nakagawa T, Busik JV, Agarwal A, Segal MS, Grant MB. Carbon monoxide and nitric oxide mediate cytoskeletal reorganization in microvascular cells via vasodilator-stimulated phosphoprotein phosphorylation: evidence for blunted responsiveness in diabetes. Diabetes. 2008 Sep;57(9):2488-94. doi: 10.2337/db08-0381. Epub 2008 Jun 16. PMID:18559661 doi:10.2337/db08-0381
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