1use

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[[Image:1use.png|left|200px]]
 
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==human VASP tetramerisation domain==
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The line below this paragraph, containing "STRUCTURE_1use", creates the "Structure Box" on the page.
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<StructureSection load='1use' size='340' side='right'caption='[[1use]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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{{STRUCTURE_1use| PDB=1use | SCENE= }}
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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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===HUMAN VASP TETRAMERISATION DOMAIN===
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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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The line below this paragraph, {{ABSTRACT_PUBMED_15569942}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1use" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15569942 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15569942}}
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==About this Structure==
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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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==See Also==
==See Also==
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*[[Group:MUZIC:Mena VASP]]
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*[[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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