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7cso

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Current revision (10:52, 27 March 2024) (edit) (undo)
 
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<StructureSection load='7cso' size='340' side='right'caption='[[7cso]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
<StructureSection load='7cso' size='340' side='right'caption='[[7cso]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7cso]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CSO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7cso]] 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=7CSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CSO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.39&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7cso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cso OCA], [https://pdbe.org/7cso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cso RCSB], [https://www.ebi.ac.uk/pdbsum/7cso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cso 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=7cso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cso OCA], [https://pdbe.org/7cso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cso RCSB], [https://www.ebi.ac.uk/pdbsum/7cso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cso ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ARHGG_MOUSE ARHGG_MOUSE]] Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 (By similarity).
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[https://www.uniprot.org/uniprot/ARHGG_MOUSE ARHGG_MOUSE] Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ephexin family guanine nucleotide exchange factors (GEFs) transfer signals from Eph tyrosine kinase receptors to Rho GTPases, which play critical roles in diverse cellular processes, as well as cancers and brain disorders. Here, we elucidate the molecular basis underlying inhibition and activation of Ephexin family RhoGEFs. The crystal structures of partially and fully autoinhibited Ephexin4 reveal that the complete autoinhibition requires both N- and C-terminal inhibitory modes, which can operate independently to impede Ras homolog family member G (RhoG) access. This double inhibition mechanism is commonly employed by other Ephexins and SGEF, another RhoGEF for RhoG. Structural, enzymatic, and cell biological analyses show that phosphorylation of a conserved tyrosine residue in its N-terminal inhibitory domain and association of PDZ proteins with its C-terminal PDZ-binding motif may respectively relieve the two autoinhibitory modes in Ephexin4. Our study provides a mechanistic framework for understanding the fine-tuning regulation of Ephexin4 GEF activity and offers possible clues for its pathological dysfunction.
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Double inhibition and activation mechanisms of Ephexin family RhoGEFs.,Zhang M, Lin L, Wang C, Zhu J Proc Natl Acad Sci U S A. 2021 Feb 23;118(8). pii: 2024465118. doi:, 10.1073/pnas.2024465118. PMID:33597305<ref>PMID:33597305</ref>
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==See Also==
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*[[Rho guanine nucleotide exchange factor 3D structures|Rho guanine nucleotide exchange factor 3D structures]]
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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 7cso" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lin, L]]
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[[Category: Mus musculus]]
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[[Category: Wang, C]]
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[[Category: Lin L]]
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[[Category: Zhang, M]]
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[[Category: Wang C]]
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[[Category: Zhu, J]]
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[[Category: Zhang M]]
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[[Category: Autoinhibition]]
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[[Category: Zhu J]]
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[[Category: Ephexin4]]
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[[Category: Gef]]
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[[Category: Signaling protein]]
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Current revision

Structure of Ephexin4 DH-PH-SH3

PDB ID 7cso

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