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2l3q

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==Structure of the prolyl trans isomer of the Crk Protein==
==Structure of the prolyl trans isomer of the Crk Protein==
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<StructureSection load='2l3q' size='340' side='right' caption='[[2l3q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2l3q' size='340' side='right'caption='[[2l3q]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2l3q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L3Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L3Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2l3q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L3Q FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2l3p|2l3p]], [[2l3s|2l3s]]</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">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</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=2l3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l3q OCA], [https://pdbe.org/2l3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l3q RCSB], [https://www.ebi.ac.uk/pdbsum/2l3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l3q ProSAT]</span></td></tr>
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<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=2l3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l3q RCSB], [http://www.ebi.ac.uk/pdbsum/2l3q PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CRK_CHICK CRK_CHICK] May mediate attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. May regulate the EFNA5-EPHA3 signaling (By similarity).
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Proline switches, controlled by cis-trans isomerization, have emerged as a particularly effective regulatory mechanism in a wide range of biological processes. Here we report the structures of both the cis and trans conformers of a proline switch in the Crk signaling protein. Proline isomerization toggles Crk between two conformations: an autoinhibitory conformation, stabilized by the intramolecular association of two tandem SH3 domains in the cis form, and an uninhibited, activated conformation promoted by the trans form. In addition to acting as a structural switch, the heterogeneous proline recruits cyclophilin A, which accelerates the interconversion rate between the isomers, thereby regulating the kinetics of Crk activation. The data provide atomic insight into the mechanisms that underpin the functionality of this binary switch and elucidate its remarkable efficiency. The results also reveal new SH3 binding surfaces, highlighting the binding versatility and expanding the noncanonical ligand repertoire of this important signaling domain.
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Structural basis for regulation of the Crk signaling protein by a proline switch.,Sarkar P, Saleh T, Tzeng SR, Birge RB, Kalodimos CG Nat Chem Biol. 2011 Jan;7(1):51-7. Epub 2010 Dec 5. PMID:21131971<ref>PMID:21131971</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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==See Also==
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</div>
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*[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Birge, R.]]
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[[Category: Large Structures]]
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[[Category: Kalodimos, C.]]
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[[Category: Birge R]]
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[[Category: Saleh, T.]]
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[[Category: Kalodimos C]]
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[[Category: Sarkar, P.]]
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[[Category: Saleh T]]
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[[Category: Tzeng, S.]]
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[[Category: Sarkar P]]
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[[Category: Adapter protein]]
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[[Category: Tzeng S]]
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[[Category: Structural protein]]
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Current revision

Structure of the prolyl trans isomer of the Crk Protein

PDB ID 2l3q

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