1egx: Difference between revisions

New page: left|200px<br /> <applet load="1egx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1egx" /> '''SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY...
 
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'''SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)'''<br />


==Overview==
==SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)==
The Ena-VASP family of proteins act as molecular adaptors linking the, cytoskeletal system to signal transduction pathways. Their N-terminal EVH1, domains use groups of exposed aromatic residues to specifically recognize, 'FPPPP' motifs found in the mammalian zyxin and vinculin proteins, and, ActA protein of the intracellular bacterium Listeria monocytogenes. Here, evidence is provided that the affinities of these EVH1-peptide, interactions are strongly dependent on the recognition of residues, flanking the core FPPPP motifs. Determination of the VASP EVH1 domain, solution structure, together with peptide library screening, measurement, of individual K(d)s by fluorescence titration, and NMR chemical shift, mapping, revealed a second affinity-determining epitope present in all, four ActA EVH1-binding motifs. The epitope was shown to interact with a, complementary hydrophobic site on the EVH1 surface and to increase, strongly the affinity of ActA for EVH1 domains. We propose that this, epitope, which is absent in the sequences of the native EVH1-interaction, partners zyxin and vinculin, may provide the pathogen with an advantage, when competing for the recruitment of the host VASP and Mena proteins in, the infected cell.
<StructureSection load='1egx' size='340' side='right'caption='[[1egx]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<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>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EGX OCA].
*[[Vasodilator-stimulated phosphoprotein|Vasodilator-stimulated phosphoprotein]]
 
== References ==
==Reference==
<references/>
Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity., Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T, EMBO J. 2000 Sep 15;19(18):4903-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10990454 10990454]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ball, L.]]
[[Category: Ball L]]
[[Category: Hafner, A.]]
[[Category: Hafner A]]
[[Category: Hof, M.]]
[[Category: Hof M]]
[[Category: Hoffmann, B.]]
[[Category: Hoffmann B]]
[[Category: Jarchau, T.]]
[[Category: Jarchau T]]
[[Category: Kuhne, R.]]
[[Category: Kuhne R]]
[[Category: Oschkinat, H.]]
[[Category: Oschkinat H]]
[[Category: Schmieder, P.]]
[[Category: Schmieder P]]
[[Category: Schneider-Mergener, J.]]
[[Category: Schneider-Mergener J]]
[[Category: Volkmer-Engert, R.]]
[[Category: Volkmer-Engert R]]
[[Category: Wahl, M.]]
[[Category: Wahl M]]
[[Category: Walter, U.]]
[[Category: Walter U]]
[[Category: evh1]]
[[Category: Z-disk]]
[[Category: nmr]]
[[Category: poly-proline-binding domain]]
[[Category: vasp-ena]]
 
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