4qj4: Difference between revisions
New page: '''Unreleased structure''' The entry 4qj4 is ON HOLD until Paper Publication Authors: Lyon, A.M., Tesmer, J.J.G. Description: Structure of a fragment of human phospholipase C-beta3 del... |
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==Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in complex with Galphaq== | |||
<StructureSection load='4qj4' size='340' side='right'caption='[[4qj4]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qj4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QJ4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4qj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qj4 OCA], [https://pdbe.org/4qj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qj4 RCSB], [https://www.ebi.ac.uk/pdbsum/4qj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qj4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GNAQ_MOUSE GNAQ_MOUSE] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro).<ref>PMID:17938235</ref> <ref>PMID:20624888</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phospholipase C beta (PLCbeta) enzymes are dramatically activated by heterotrimeric G proteins. Central to this response is the robust autoinhibition of PLCbeta by the X-Y linker region within its catalytic core and by the Halpha2' helix in the C-terminal extension of the enzyme. The molecular mechanism of each and their mutual dependence are poorly understood. Herein, it is shown that distinct regions within the X-Y linker have specific roles in regulating activity. Most important, an acidic stretch within the linker stabilizes a lid that occludes the active site, consistent with crystal structures of variants lacking this region. Inhibition by the Halpha2' helix is independent of the X-Y linker and likely regulates activity by limiting membrane interaction of the catalytic core. Full activation of PLCbeta thus requires multiple independent molecular events induced by membrane association of the catalytic core and by the binding of regulatory proteins. | |||
Molecular Mechanisms of Phospholipase C beta3 Autoinhibition.,Lyon AM, Begley JA, Manett TD, Tesmer JJ Structure. 2014 Nov 25. pii: S0969-2126(14)00335-9. doi:, 10.1016/j.str.2014.10.008. PMID:25435326<ref>PMID:25435326</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4qj4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phospholipase C|Phospholipase C]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Lyon AM]] | |||
[[Category: Tesmer JJG]] | |||
Latest revision as of 20:32, 20 September 2023
Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in complex with GalphaqStructure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in complex with Galphaq
Structural highlights
FunctionGNAQ_MOUSE Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro).[1] [2] Publication Abstract from PubMedPhospholipase C beta (PLCbeta) enzymes are dramatically activated by heterotrimeric G proteins. Central to this response is the robust autoinhibition of PLCbeta by the X-Y linker region within its catalytic core and by the Halpha2' helix in the C-terminal extension of the enzyme. The molecular mechanism of each and their mutual dependence are poorly understood. Herein, it is shown that distinct regions within the X-Y linker have specific roles in regulating activity. Most important, an acidic stretch within the linker stabilizes a lid that occludes the active site, consistent with crystal structures of variants lacking this region. Inhibition by the Halpha2' helix is independent of the X-Y linker and likely regulates activity by limiting membrane interaction of the catalytic core. Full activation of PLCbeta thus requires multiple independent molecular events induced by membrane association of the catalytic core and by the binding of regulatory proteins. Molecular Mechanisms of Phospholipase C beta3 Autoinhibition.,Lyon AM, Begley JA, Manett TD, Tesmer JJ Structure. 2014 Nov 25. pii: S0969-2126(14)00335-9. doi:, 10.1016/j.str.2014.10.008. PMID:25435326[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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