4y93
From Proteopedia
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| - | ''' | + | ==Crystal structure of the PH-TH-kinase construct of Bruton's tyrosine kinase (Btk)== |
| + | <StructureSection load='4y93' size='340' side='right' caption='[[4y93]], [[Resolution|resolution]] 1.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4y93]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y93 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=746:4-TERT-BUTYL-N-[2-METHYL-3-(4-METHYL-6-{[4-(MORPHOLIN-4-YLCARBONYL)PHENYL]AMINO}-5-OXO-4,5-DIHYDROPYRAZIN-2-YL)PHENYL]BENZAMIDE'>746</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y94|4y94]], [[4y95|4y95]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span></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=4y93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y93 RCSB], [http://www.ebi.ac.uk/pdbsum/4y93 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bruton's tyrosine kinase (Btk), a Tec-family tyrosine kinase, is essential for B-cell function. We present crystallographic and biochemical analyses of Btk, which together reveal molecular details of its autoinhibition and activation. Autoinhibited Btk adopts a compact conformation like that of inactive c-Src and c-Abl. A lipid-binding PH-TH module, unique to Tec kinases, acts in conjunction with the SH2 and SH3 domains to stabilize the inactive conformation. In addition to the expected activation of Btk by membranes containing phosphatidylinositol triphosphate (PIP3), we found that inositol hexakisphosphate (IP6), a soluble signaling molecule found in both animal and plant cells, also activates Btk. This activation is a consequence of a transient PH-TH dimerization induced by IP6, which promotes transphosphorylation of the kinase domains. Sequence comparisons with other Tec-family kinases suggest that activation by IP6 is unique to Btk. | ||
| - | + | Autoinhibition of Bruton's tyrosine kinase (Btk) and activation by soluble inositol hexakisphosphate.,Wang Q, Vogan EM, Nocka LM, Rosen CE, Zorn JA, Harrison SC, Kuriyan J Elife. 2015 Feb 20;4. doi: 10.7554/eLife.06074. PMID:25699547<ref>PMID:25699547</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Non-specific protein-tyrosine kinase]] | ||
[[Category: Kuriyan, J]] | [[Category: Kuriyan, J]] | ||
[[Category: Wang, Q]] | [[Category: Wang, Q]] | ||
| + | [[Category: Btk]] | ||
| + | [[Category: Ph-th]] | ||
| + | [[Category: Tyrosine kinase]] | ||
Revision as of 12:02, 18 March 2015
Crystal structure of the PH-TH-kinase construct of Bruton's tyrosine kinase (Btk)
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