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2l3p

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==Structure of the prolyl cis isomer of the Crk Protein==
==Structure of the prolyl cis isomer of the Crk Protein==
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<StructureSection load='2l3p' size='340' side='right' caption='[[2l3p]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2l3p' size='340' side='right'caption='[[2l3p]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2l3p]] 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=2L3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L3P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2l3p]] 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=2L3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L3P FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2l3q|2l3q]], [[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=2l3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l3p OCA], [https://pdbe.org/2l3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l3p RCSB], [https://www.ebi.ac.uk/pdbsum/2l3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l3p 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=2l3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l3p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l3p RCSB], [http://www.ebi.ac.uk/pdbsum/2l3p PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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</div>
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==See Also==
==See Also==
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*[[Adapter molecule crk|Adapter molecule crk]]
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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 G]]
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[[Category: Birge R]]
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[[Category: Saleh, T]]
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[[Category: Kalodimos CG]]
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[[Category: Sarkar, P]]
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[[Category: Saleh T]]
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[[Category: Tzeng, S R]]
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[[Category: Sarkar P]]
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[[Category: Adapter protein]]
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[[Category: Tzeng SR]]
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[[Category: Structural protein]]
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Current revision

Structure of the prolyl cis isomer of the Crk Protein

PDB ID 2l3p

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