4y95: Difference between revisions
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==Crystal structure of the kinase domain of Bruton's tyrosine kinase with mutations in the activation loop== | ==Crystal structure of the kinase domain of Bruton's tyrosine kinase with mutations in the activation loop== | ||
<StructureSection load='4y95' size='340' side='right' caption='[[4y95]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4y95' size='340' side='right' caption='[[4y95]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y93|4y93]], [[4y94|4y94]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y93|4y93]], [[4y94|4y94]]</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='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=4y95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y95 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y95 RCSB], [http://www.ebi.ac.uk/pdbsum/4y95 PDBsum]</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=4y95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y95 OCA], [http://pdbe.org/4y95 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y95 RCSB], [http://www.ebi.ac.uk/pdbsum/4y95 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y95 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4y95" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 04:54, 10 March 2017
Crystal structure of the kinase domain of Bruton's tyrosine kinase with mutations in the activation loopCrystal structure of the kinase domain of Bruton's tyrosine kinase with mutations in the activation loop
Structural highlights
Publication Abstract from PubMedBruton'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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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