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1qc6

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[[Image:1qc6.gif|left|200px]]
 
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{{Structure
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==EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide==
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|PDB= 1qc6 |SIZE=350|CAPTION= <scene name='initialview01'>1qc6</scene>, resolution 2.6&Aring;
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<StructureSection load='1qc6' size='340' side='right'caption='[[1qc6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1qc6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QC6 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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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=1qc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qc6 OCA], [https://pdbe.org/1qc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qc6 RCSB], [https://www.ebi.ac.uk/pdbsum/1qc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qc6 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qc6 OCA], [http://www.ebi.ac.uk/pdbsum/1qc6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qc6 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/EVL_MOUSE EVL_MOUSE] Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.<ref>PMID:10945997</ref> <ref>PMID:10087267</ref>
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== Evolutionary Conservation ==
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'''EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qc/1qc6_consurf.spt"</scriptWhenChecked>
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The Ena-VASP homology (EVH1) domain is a protein interaction module found in several proteins that are involved in transducing migratory and morphological signals into cytoskeletal reorganization. EVH1 specifically recognizes proline-rich sequences in its binding partners and directs the localization and formation of multicomponent assemblies involved in actin-based motile processes and neural development. The structure of the complex between an EVH1 domain and the target peptide sequence EFPPPPT identifies the interactions responsible for recognition and distinguishes it from other proline-rich binding modules, including SH3 and WW domains. Surprisingly, the EVH1 domain has structural similarity to pleckstrin homology (PH), phosphotyrosine-binding (PTB) and ran-binding (RanBD) domains.
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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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==About this Structure==
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</jmolCheckbox>
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1QC6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC6 OCA].
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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=1qc6 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function., Fedorov AA, Fedorov E, Gertler F, Almo SC, Nat Struct Biol. 1999 Jul;6(7):661-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10404224 10404224]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Almo SC]]
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[[Category: Almo, S C.]]
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[[Category: Fedorov AA]]
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[[Category: Fedorov, A A.]]
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[[Category: Fedorov EV]]
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[[Category: Fedorov, E V.]]
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[[Category: Gertler FB]]
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[[Category: Gertler, F B.]]
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[[Category: actin-based cell motility]]
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[[Category: an incomplete seven stranded anti-parallel beta barrel closed by an alpha helix]]
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[[Category: evh1 domain]]
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[[Category: interaction module]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:39 2008''
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Current revision

EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide

PDB ID 1qc6

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