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4js0

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==Complex of Cdc42 with the CRIB-PR domain of IRSp53==
==Complex of Cdc42 with the CRIB-PR domain of IRSp53==
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<StructureSection load='4js0' size='340' side='right' caption='[[4js0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='4js0' size='340' side='right'caption='[[4js0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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[[4js0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JS0 OCA]. <br>
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<table><tr><td colspan='2'>[[4js0]] is a 2 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=4JS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JS0 FirstGlance]. <br>
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<b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene><br>
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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]] 1.9&#8491;</td></tr>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene></td></tr>
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<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4js0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4js0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4js0 RCSB], [http://www.ebi.ac.uk/pdbsum/4js0 PDBsum]</span><br>
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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=4js0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4js0 OCA], [https://pdbe.org/4js0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4js0 RCSB], [https://www.ebi.ac.uk/pdbsum/4js0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4js0 ProSAT]</span></td></tr>
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== Publication Abstract from PubMed ==
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</table>
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The Rho family GTPase effector IRSp53 has essential roles in filopodia formation and neuronal development, but its regulatory mechanism is poorly understood. IRSp53 contains a membrane-binding BAR domain followed by an unconventional CRIB motif that overlaps with a proline-rich region (CRIB-PR) and an SH3 domain that recruits actin cytoskeleton effectors. Using a fluorescence reporter assay, we show that human IRSp53 adopts a closed inactive conformation that opens synergistically with the binding of human Cdc42 to the CRIB-PR and effector proteins, such as the tumor-promoting factor Eps8, to the SH3 domain. The crystal structure of Cdc42 bound to the CRIB-PR reveals a new mode of effector binding to Rho family GTPases. Structure-inspired mutations disrupt autoinhibition and Cdc42 binding in vitro and decouple Cdc42- and IRSp53-dependent filopodia formation in cells. The data support a combinatorial mechanism of IRSp53 activation.
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== Function ==
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[https://www.uniprot.org/uniprot/CDC42_HUMAN CDC42_HUMAN] Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration.<ref>PMID:14978216</ref> <ref>PMID:15642749</ref> <ref>PMID:17038317</ref>
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Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors.,Kast DJ, Yang C, Disanza A, Boczkowska M, Madasu Y, Scita G, Svitkina T, Dominguez R Nat Struct Mol Biol. 2014 Mar 2. doi: 10.1038/nsmb.2781. PMID:24584464<ref>PMID:24584464</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Dominguez, R.]]
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[[Category: Large Structures]]
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[[Category: Kast, D J.]]
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[[Category: Dominguez R]]
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[[Category: Crib domain]]
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[[Category: Kast DJ]]
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[[Category: Cytoskeleton regulation]]
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[[Category: Gtpase binding domain]]
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[[Category: Signaling protein-signaling protein complex]]
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Current revision

Complex of Cdc42 with the CRIB-PR domain of IRSp53

PDB ID 4js0

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