2iyb

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[[Image:2iyb.gif|left|200px]]
 
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{{Structure
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==Structure of complex between the 3rd LIM domain of TES and the EVH1 domain of Mena==
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|PDB= 2iyb |SIZE=350|CAPTION= <scene name='initialview01'>2iyb</scene>, resolution 2.350&Aring;
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<StructureSection load='2iyb' size='340' side='right'caption='[[2iyb]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+E'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+E'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+E'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+F'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Chain+F'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+G'>AC6</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Chain+G'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Chain+H'>AC8</scene> and <scene name='pdbsite=AC9:Zn+Binding+Site+For+Chain+H'>AC9</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2iyb]] is a 8 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=2IYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IYB 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]] 2.35&#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=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=2iyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyb OCA], [https://pdbe.org/2iyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iyb RCSB], [https://www.ebi.ac.uk/pdbsum/2iyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyb ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF COMPLEX BETWEEN THE 3RD LIM DOMAIN OF TES AND THE EVH1 DOMAIN OF MENA'''
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== Function ==
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[https://www.uniprot.org/uniprot/ENAH_HUMAN ENAH_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 and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity).<ref>PMID:11696321</ref> <ref>PMID:18158903</ref>
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== Evolutionary Conservation ==
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==Overview==
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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/iy/2iyb_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=2iyb 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 ==
The intracellular targeting of Ena/VASP family members is achieved via the interaction of their EVH1 domain with FPPPP sequence motifs found in a variety of cytoskeletal proteins, including lamellipodin, vinculin, and zyxin. Here we show that the LIM3 domain of Tes, which lacks the FPPPP motif, binds to the EVH1 domain of Mena, but not to those of VASP or Evl. The structure of the LIM3:EVH1 complex reveals that Tes occludes the FPPPP-binding site and competes with FPPPP-containing proteins for EVH1 binding. Structure-based gain-of-function experiments define the molecular basis for the specificity of the Tes-Mena interaction. Consistent with in vitro observations, the LIM3 domain displaces Mena, but not VASP, from the leading edge and focal adhesions. It also regulates cell migration through a Mena-dependent mechanism. Our observations identify Tes as an atypical EVH1 binding partner and a regulator specific to a single Ena/VASP family member.
The intracellular targeting of Ena/VASP family members is achieved via the interaction of their EVH1 domain with FPPPP sequence motifs found in a variety of cytoskeletal proteins, including lamellipodin, vinculin, and zyxin. Here we show that the LIM3 domain of Tes, which lacks the FPPPP motif, binds to the EVH1 domain of Mena, but not to those of VASP or Evl. The structure of the LIM3:EVH1 complex reveals that Tes occludes the FPPPP-binding site and competes with FPPPP-containing proteins for EVH1 binding. Structure-based gain-of-function experiments define the molecular basis for the specificity of the Tes-Mena interaction. Consistent with in vitro observations, the LIM3 domain displaces Mena, but not VASP, from the leading edge and focal adhesions. It also regulates cell migration through a Mena-dependent mechanism. Our observations identify Tes as an atypical EVH1 binding partner and a regulator specific to a single Ena/VASP family member.
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==About this Structure==
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Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding.,Boeda B, Briggs DC, Higgins T, Garvalov BK, Fadden AJ, McDonald NQ, Way M Mol Cell. 2007 Dec 28;28(6):1071-82. PMID:18158903<ref>PMID:18158903</ref>
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2IYB is a [[Protein complex]] structure of sequences 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=2IYB OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding., Boeda B, Briggs DC, Higgins T, Garvalov BK, Fadden AJ, McDonald NQ, Way M, Mol Cell. 2007 Dec 28;28(6):1071-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18158903 18158903]
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</div>
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<div class="pdbe-citations 2iyb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Briggs, D C.]]
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[[Category: Briggs DC]]
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[[Category: Mcdonald, N Q.]]
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[[Category: McDonald NQ]]
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[[Category: ZN]]
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[[Category: actin-binding]]
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[[Category: alternative splicing]]
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[[Category: coiled coil]]
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[[Category: cytoskeleton]]
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[[Category: lim domain]]
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[[Category: metal-binding]]
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[[Category: phosphorylation]]
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[[Category: sh3-binding]]
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[[Category: tumour supressor lim domain evh1 domain cell motility]]
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[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:34:59 2008''
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Current revision

Structure of complex between the 3rd LIM domain of TES and the EVH1 domain of Mena

PDB ID 2iyb

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