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6pbc

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Current revision (14:54, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6pbc' size='340' side='right'caption='[[6pbc]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
<StructureSection load='6pbc' size='340' side='right'caption='[[6pbc]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[6pbc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6PBC FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.46&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pbc OCA], [https://pdbe.org/6pbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pbc RCSB], [https://www.ebi.ac.uk/pdbsum/6pbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pbc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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]
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[https://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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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==See Also==
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*[[Phospholipase C|Phospholipase C]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6pbc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hajicek, N]]
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[[Category: Rattus norvegicus]]
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[[Category: Sondek, J]]
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[[Category: Hajicek N]]
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[[Category: 1-phosphatidylinositol 4]]
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[[Category: Sondek J]]
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[[Category: 5-bisphosphate phosphodiesterase gamma-1]]
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[[Category: Hydrolase]]
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Current revision

Structural basis for the activation of PLC-gamma isozymes by phosphorylation and cancer-associated mutations

PDB ID 6pbc

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