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{{STRUCTURE_4gnk|  PDB=4gnk  |  SCENE=  }}
===Crystal structure of Galphaq in complex with full-length human PLCbeta3===
{{ABSTRACT_PUBMED_23377541}}


==Function==
==Crystal structure of Galphaq in complex with full-length human PLCbeta3==
[[http://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> [[http://www.uniprot.org/uniprot/PLCB3_HUMAN PLCB3_HUMAN]] The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.  
<StructureSection load='4gnk' size='340' side='right'caption='[[4gnk]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gnk]] is a 5 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=4GNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GNK 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]] 4&#8491;</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=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=4gnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gnk OCA], [https://pdbe.org/4gnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gnk RCSB], [https://www.ebi.ac.uk/pdbsum/4gnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gnk 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) is directly activated by Galphaq, but the molecular basis for how its distal C-terminal domain (CTD) contributes to maximal activity is poorly understood. Herein we present both the crystal structure and cryo-EM three-dimensional reconstructions of human full-length PLCbeta3 in complex with mouse Galphaq. The distal CTD forms an extended monomeric helical bundle consisting of three antiparallel segments with structural similarity to membrane-binding bin-amphiphysin-Rvs (BAR) domains. Sequence conservation of the distal CTD suggests putative membrane and protein interaction sites, the latter of which bind the N-terminal helix of Galphaq in both the crystal structure and cryo-EM reconstructions. Functional analysis suggests that the distal CTD has roles in membrane targeting and in optimizing the orientation of the catalytic core at the membrane for maximal rates of lipid hydrolysis.


==About this Structure==
Full-length Galpha(q)-phospholipase C-beta3 structure reveals interfaces of the C-terminal coiled-coil domain.,Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ Nat Struct Mol Biol. 2013 Mar;20(3):355-62. doi: 10.1038/nsmb.2497. Epub 2013 Feb, 3. PMID:23377541<ref>PMID:23377541</ref>
[[4gnk]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GNK OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:023377541</ref><references group="xtra"/><references/>
</div>
<div class="pdbe-citations 4gnk" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Phospholipase C|Phospholipase C]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Lyon AM]]
[[Category: Lyon, A M.]]
[[Category: Tesmer JJG]]
[[Category: Tesmer, J J.G.]]
[[Category: C2 domain]]
[[Category: Calcium binding]]
[[Category: Coiled-coil domain]]
[[Category: Ef hand]]
[[Category: G-protein signaling]]
[[Category: Gtp binding]]
[[Category: Gtp hydrolysis]]
[[Category: Gtp-binding protein alpha subunit]]
[[Category: Gtp-binding protein-hydrolase complex]]
[[Category: Hydrolase]]
[[Category: Lipase]]
[[Category: Membrane targeting]]
[[Category: Ph domain]]
[[Category: Phospholipase]]
[[Category: Phospholipase c beta]]
[[Category: Phospholipid]]
[[Category: Tim barrel domain]]
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