1use

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{{STRUCTURE_1use| PDB=1use | SCENE= }}
 
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===HUMAN VASP TETRAMERISATION DOMAIN===
 
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{{ABSTRACT_PUBMED_15569942}}
 
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==About this Structure==
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==human VASP tetramerisation domain==
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[[1use]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USE OCA].
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<StructureSection load='1use' size='340' side='right'caption='[[1use]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1use]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USE 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">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</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=1use FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1use OCA], [https://pdbe.org/1use PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1use RCSB], [https://www.ebi.ac.uk/pdbsum/1use PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1use ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/us/1use_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1use ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-A resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed alpha-helical coiled-coil structure with a similar degree of supercoiling as found in the widespread left-handed coiled coils with heptad repeats. The basis for the right-handed geometry of VASP TD is a 15-residue repeat in its amino acid sequence, which reveals a characteristic pattern of hydrophobic residues. Hydrophobic interactions and a network of salt bridges render VASP TD highly thermostable with a melting point of 120 degrees C.
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The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.,Kuhnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17027-32. Epub 2004 Nov 29. PMID:15569942<ref>PMID:15569942</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1use" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Group:MUZIC:Mena VASP|MUZIC:Mena VASP]]
 
*[[Vasodilator-stimulated phosphoprotein|Vasodilator-stimulated phosphoprotein]]
*[[Vasodilator-stimulated phosphoprotein|Vasodilator-stimulated phosphoprotein]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015569942</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Jarchau, T.]]
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[[Category: Large Structures]]
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[[Category: Kuhnel, K.]]
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[[Category: Jarchau T]]
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[[Category: Schlichting, I.]]
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[[Category: Kuhnel K]]
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[[Category: Strelkov, S V.]]
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[[Category: Schlichting I]]
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[[Category: Walter, U.]]
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[[Category: Strelkov SV]]
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[[Category: Wittinghofer, A.]]
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[[Category: Walter U]]
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[[Category: Wolf, E.]]
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[[Category: Wittinghofer A]]
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[[Category: Signaling protein]]
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[[Category: Wolf E]]
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[[Category: Z-disk]]

Current revision

human VASP tetramerisation domain

PDB ID 1use

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