2lqn
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2lqn is ON HOLD Authors: Jankowski, W., Saleh, T., Kalodimos, C. Description: Solution structure of CRKL) |
|||
| (11 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of CRKL== | |
| + | <StructureSection load='2lqn' size='340' side='right'caption='[[2lqn]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lqn]] 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=2LQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqn OCA], [https://pdbe.org/2lqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqn RCSB], [https://www.ebi.ac.uk/pdbsum/2lqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqn 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 2lqn" 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 CRKL
| |||||||||||
