3a8q

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Current revision (13:59, 13 March 2024) (edit) (undo)
 
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<StructureSection load='3a8q' size='340' side='right'caption='[[3a8q]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='3a8q' size='340' side='right'caption='[[3a8q]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3a8q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A8Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3a8q]] 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=3A8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A8Q FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a8n|3a8n]], [[3a8p|3a8p]]</div></td></tr>
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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]] 3.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tiam2, Kiaa2016, Stef ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8q OCA], [https://pdbe.org/3a8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a8q RCSB], [https://www.ebi.ac.uk/pdbsum/3a8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8q 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=3a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8q OCA], [https://pdbe.org/3a8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a8q RCSB], [https://www.ebi.ac.uk/pdbsum/3a8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TIAM2_MOUSE TIAM2_MOUSE]] Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane.<ref>PMID:10364228</ref> <ref>PMID:11707441</ref> <ref>PMID:12912917</ref> <ref>PMID:14550769</ref> <ref>PMID:17320046</ref>
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[https://www.uniprot.org/uniprot/TIAM2_MOUSE TIAM2_MOUSE] Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane.<ref>PMID:10364228</ref> <ref>PMID:11707441</ref> <ref>PMID:12912917</ref> <ref>PMID:14550769</ref> <ref>PMID:17320046</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=3a8q 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=3a8q ConSurf].
<div style="clear:both"></div>
<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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Tiam1 and Tiam2 (Tiam1/2) are guanine nucleotide-exchange factors that possess the PH-CC-Ex (pleckstrin homology, coiled coil and extra) region that mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. Crystal structures of the PH-CC-Ex regions revealed a single globular domain, PHCCEx domain, comprising a conventional PH subdomain associated with an antiparallel coiled coil of CC subdomain and a novel three-helical globular Ex subdomain. The PH subdomain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. Mutational and binding studies indicated that CC and Ex subdomains form a positively charged surface for protein binding. We identified two unique acidic sequence motifs in Tiam1/2-interacting proteins for binding to PHCCEx domain, Motif-I in CD44 and ephrinB's and the NMDA receptor, and Motif-II in Par3 and JIP2. Our results suggest the molecular basis by which the Tiam1/2 PHCCEx domain facilitates dual binding to membranes and signalling proteins.
 
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The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.,Terawaki S, Kitano K, Mori T, Zhai Y, Higuchi Y, Itoh N, Watanabe T, Kaibuchi K, Hakoshima T EMBO J. 2010 Jan 6;29(1):236-50. Epub 2009 Nov 5. PMID:19893486<ref>PMID:19893486</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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<div class="pdbe-citations 3a8q" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Hakoshima, T]]
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[[Category: Hakoshima T]]
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[[Category: Higuchi, Y]]
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[[Category: Higuchi Y]]
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[[Category: Itoh, N]]
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[[Category: Itoh N]]
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[[Category: Kaibuchi, K]]
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[[Category: Kaibuchi K]]
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[[Category: Kitano, K]]
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[[Category: Kitano K]]
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[[Category: Mori, T]]
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[[Category: Mori T]]
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[[Category: Terawaki, S]]
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[[Category: Terawaki S]]
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[[Category: Watanabe, T]]
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[[Category: Watanabe T]]
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[[Category: Zhai, Y]]
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[[Category: Zhai Y]]
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[[Category: Alternative splicing]]
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[[Category: Cell projection]]
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[[Category: Coiled coil]]
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[[Category: Cytoplasm]]
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[[Category: Guanine nucleotide exchange factor]]
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[[Category: Guanine-nucleotide releasing factor]]
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[[Category: Lipoprotein]]
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[[Category: Myristate]]
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[[Category: Phosphoprotein]]
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[[Category: Signaling protein]]
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Current revision

Low-resolution crystal structure of the Tiam2 PHCCEx domain

PDB ID 3a8q

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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