2lqw
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2lqw is ON HOLD until sometime in the future Authors: Jankowski, W., Saleh, T., Kalodimos, C. Description: Solution structure of phosphorylated CRK...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of phosphorylated CRKL== | |
| + | <StructureSection load='2lqw' size='340' side='right'caption='[[2lqw]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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'>[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> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CRKL_HUMAN CRKL_HUMAN] May mediate the transduction of intracellular signals. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:22581121</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2lqw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jankowski W]] | ||
| + | [[Category: Kalodimos C]] | ||
| + | [[Category: Saleh T]] | ||
Current revision
Solution structure of phosphorylated CRKL
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