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| - | {{Large structure}}
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| | ==Solution structure of phosphorylated CRKL== | | ==Solution structure of phosphorylated CRKL== |
| - | <StructureSection load='2lqw' size='340' side='right' caption='[[2lqw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lqw' size='340' side='right'caption='[[2lqw]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lqw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LQW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQW FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRKL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></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=2lqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqw OCA], [http://pdbe.org/2lqw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lqw RCSB], [http://www.ebi.ac.uk/pdbsum/2lqw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqw 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=2lqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqw OCA], [https://pdbe.org/2lqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqw RCSB], [https://www.ebi.ac.uk/pdbsum/2lqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | {{Large structure}} | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CRKL_HUMAN CRKL_HUMAN]] May mediate the transduction of intracellular signals. | + | [https://www.uniprot.org/uniprot/CRKL_HUMAN CRKL_HUMAN] May mediate the transduction of intracellular signals. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Jankowski, W]] | + | [[Category: Large Structures]] |
| - | [[Category: Kalodimos, C]] | + | [[Category: Jankowski W]] |
| - | [[Category: Saleh, T]] | + | [[Category: Kalodimos C]] |
| - | [[Category: Oncogene homolog]] | + | [[Category: Saleh T]] |
| - | [[Category: Pcrkl]]
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| - | [[Category: Sh2]]
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| - | [[Category: Sh3]]
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| - | [[Category: Signaling protein]]
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| - | [[Category: V-crk sarcoma virus ct10]]
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| Structural highlights
Function
CRKL_HUMAN May mediate the transduction of intracellular signals.
Publication Abstract from PubMed
CrkL is a key signaling protein that mediates the leukemogenic activity of Bcr-Abl. CrkL is thought to adopt a structure that is similar to that of its CrkII homolog. The two proteins share high sequence identity and indistinguishable ligand binding preferences, yet they have distinct physiological roles. Here we show that the structures of CrkL and phosphorylated CrkL are markedly different than the corresponding structures of CrkII. As a result, the binding activities of the Src homology 2 and Src homology 3 domains in the two proteins are regulated in a distinct manner and to a different extent. The different structural architecture of CrkL and CrkII may account for their distinct functional roles. The data show that CrkL forms a constitutive complex with Abl, thus explaining the strong preference of Bcr-Abl for CrkL. The results also highlight how the structural organization of the modular domains in adaptor proteins can control signaling outcome.
Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII.,Jankowski W, Saleh T, Pai MT, Sriram G, Birge RB, Kalodimos CG Nat Chem Biol. 2012 May 13;8(6):590-6. doi: 10.1038/nchembio.954. PMID:22581121[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jankowski W, Saleh T, Pai MT, Sriram G, Birge RB, Kalodimos CG. Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII. Nat Chem Biol. 2012 May 13;8(6):590-6. doi: 10.1038/nchembio.954. PMID:22581121 doi:10.1038/nchembio.954
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