6pbc
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural basis for the activation of PLC-gamma isozymes by phosphorylation and cancer-associated mutations== | |
| + | <StructureSection load='6pbc' size='340' side='right'caption='[[6pbc]], [[Resolution|resolution]] 2.46Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6pbc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PBC FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6pbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pbc OCA], [http://pdbe.org/6pbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pbc RCSB], [http://www.ebi.ac.uk/pdbsum/6pbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pbc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/G3V845_RAT G3V845_RAT]] Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades.[PIRNR:PIRNR000952] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Direct activation of the human phospholipase C-g isozymes (PLC-g1, -g2) by tyrosine phosphorylation is fundamental to the control of diverse biological processes, including chemotaxis, platelet aggregation, and adaptive immunity. In turn, aberrant activation of PLC-g1 and PLC-g2 is implicated in inflammation, autoimmunity, and cancer. Although structures of isolated domains from PLC-g isozymes are available, these structures are insufficient to define how release of basal autoinhibition is coupled to phosphorylation-dependent enzyme activation. Here we describe the first high-resolution structure of a full-length PLC-g isozyme and use it to underpin a detailed model of their membrane-dependent regulation. Notably, an interlinked set of regulatory domains integrates basal autoinhibition, tyrosine kinase engagement, and additional scaffolding functions with the phosphorylation-dependent, allosteric control of phospholipase activation. The model also explains why mutant forms of the PLC-g isozymes found in several cancers have a wide spectrum of activities, and highlights how these activities are tuned during disease. | ||
| - | + | Structural basis for the activation of PLC-gamma isozymes by phosphorylation and cancer-associated mutations.,Hajicek N, Keith NC, Siraliev-Perez E, Temple BRS, Huang W, Zhang Q, Harden TK, Sondek J Elife. 2019 Dec 31;8. pii: 51700. doi: 10.7554/eLife.51700. PMID:31889510<ref>PMID:31889510</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6pbc" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Hajicek, N]] | [[Category: Hajicek, N]] | ||
| + | [[Category: Sondek, J]] | ||
| + | [[Category: 1-phosphatidylinositol 4]] | ||
| + | [[Category: 5-bisphosphate phosphodiesterase gamma-1]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 07:36, 8 January 2020
Structural basis for the activation of PLC-gamma isozymes by phosphorylation and cancer-associated mutations
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