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| ==Crystal structure of the active dimer of zebrafish PlexinC1 cytoplasmic region== | | ==Crystal structure of the active dimer of zebrafish PlexinC1 cytoplasmic region== |
| <StructureSection load='4m8m' size='340' side='right' caption='[[4m8m]], [[Resolution|resolution]] 3.31Å' scene=''> | | <StructureSection load='4m8m' size='340' side='right'caption='[[4m8m]], [[Resolution|resolution]] 3.31Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4m8m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M8M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M8M FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4m8m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M8M FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m8n|4m8n]]</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.307Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Plexin C1, plxnc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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=4m8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m8m OCA], [https://pdbe.org/4m8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m8m RCSB], [https://www.ebi.ac.uk/pdbsum/4m8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m8m ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m8m OCA], [http://pdbe.org/4m8m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m8m RCSB], [http://www.ebi.ac.uk/pdbsum/4m8m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m8m ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q5RGW1_DANRE Q5RGW1_DANRE] |
| Plexins are cell surface receptors that bind semaphorins and transduce signals for regulating neuronal axon guidance and other processes. Plexin signaling depends on their cytoplasmic GTPase activating protein (GAP) domain, which specifically inactivates the Ras homolog Rap through an ill-defined non-canonical catalytic mechanism. The plexin GAP is activated by semaphorin-induced dimerization, the structural basis for which remained unknown. Here we present the crystal structures of the active dimer of zebrafish PlexinC1 cytoplasmic region in the apo state and in complex with Rap. The structures show that the dimerization induces a large-scale conformational change in plexin, which opens the GAP active site to allow Rap binding. Plexin stabilizes the switch II region of Rap in an unprecedented conformation, bringing Gln63 in Rap into the active site for catalyzing GTP hydrolysis. The structures also explain the unique Rap-specificity of plexins. Mutational analyses support that these mechanisms underlie plexin activation and signaling. DOI:http://dx.doi.org/10.7554/eLife.01279.001.
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| Structural basis for activation and non-canonical catalysis of the Rap GTPase activating protein domain of plexin.,Wang Y, Pascoe HG, Brautigam CA, He H, Zhang X Elife. 2013 Oct 1;2:e01279. doi: 10.7554/eLife.01279. PMID:24137545<ref>PMID:24137545</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4m8m" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Gcn4|Gcn4]] | | *[[Gcn4 3D Structures|Gcn4 3D Structures]] |
| == References ==
| | *[[Gnc4 3D Structures|Gnc4 3D Structures]] |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Brachidanio rerio]] | | [[Category: Danio rerio]] |
| [[Category: Pascoe, H G]] | | [[Category: Large Structures]] |
| [[Category: Wang, Y]] | | [[Category: Pascoe HG]] |
| [[Category: Zhang, X]] | | [[Category: Wang Y]] |
| [[Category: Gap for rap gtpase]] | | [[Category: Zhang X]] |
| [[Category: Membrane]]
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| [[Category: Rap]]
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| [[Category: Rasgap-like fold]]
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| [[Category: Signaling protein]]
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