1qc6
From Proteopedia
(Difference between revisions)
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<StructureSection load='1qc6' size='340' side='right'caption='[[1qc6]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1qc6' size='340' side='right'caption='[[1qc6]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1qc6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| + | <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> | ||
<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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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:10404224<ref>PMID:10404224</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1qc6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Almo | + | [[Category: Almo SC]] |
| - | [[Category: Fedorov | + | [[Category: Fedorov AA]] |
| - | [[Category: Fedorov | + | [[Category: Fedorov EV]] |
| - | [[Category: Gertler | + | [[Category: Gertler FB]] |
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Revision as of 06:03, 17 April 2024
EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide
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