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4qj4

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Revision as of 17:16, 4 January 2017

Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in complex with Galphaq

Structural highlights

4qj4 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	4qj3, 4qj5
Activity:	Phosphoinositide phospholipase C, with EC number 3.1.4.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2] [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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shi G, Partida-Sanchez S, Misra RS, Tighe M, Borchers MT, Lee JJ, Simon MI, Lund FE. Identification of an alternative G{alpha}q-dependent chemokine receptor signal transduction pathway in dendritic cells and granulocytes. J Exp Med. 2007 Oct 29;204(11):2705-18. Epub 2007 Oct 15. PMID:17938235 doi:10.1084/jem.20071267
↑ Misra RS, Shi G, Moreno-Garcia ME, Thankappan A, Tighe M, Mousseau B, Kusser K, Becker-Herman S, Hudkins KL, Dunn R, Kehry MR, Migone TS, Marshak-Rothstein A, Simon M, Randall TD, Alpers CE, Liggitt D, Rawlings DJ, Lund FE. G alpha q-containing G proteins regulate B cell selection and survival and are required to prevent B cell-dependent autoimmunity. J Exp Med. 2010 Aug 2;207(8):1775-89. doi: 10.1084/jem.20092735. Epub 2010 Jul, 12. PMID:20624888 doi:10.1084/jem.20092735
↑ Lyon AM, Begley JA, Manett TD, Tesmer JJ. Molecular Mechanisms of Phospholipase C beta3 Autoinhibition. Structure. 2014 Nov 25. pii: S0969-2126(14)00335-9. doi:, 10.1016/j.str.2014.10.008. PMID:25435326 doi:http://dx.doi.org/10.1016/j.str.2014.10.008

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4qj4"

@@ Line 1: / Line 1: @@
 ==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]] 3.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qj3|4qj3]], [[4qj5|4qj5]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] </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=4qj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qj4 RCSB], [http://www.ebi.ac.uk/pdbsum/4qj4 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=4qj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qj4 OCA], [http://pdbe.org/4qj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qj4 RCSB], [http://www.ebi.ac.uk/pdbsum/4qj4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qj4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, 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/>

4qj4

From Proteopedia

Revision as of 17:16, 4 January 2017

Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in complex with Galphaq

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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