4gnk
From Proteopedia
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{{STRUCTURE_4gnk| PDB=4gnk | SCENE= }} | {{STRUCTURE_4gnk| PDB=4gnk | SCENE= }} | ||
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===Crystal structure of Galphaq in complex with full-length human PLCbeta3=== | ===Crystal structure of Galphaq in complex with full-length human PLCbeta3=== | ||
+ | {{ABSTRACT_PUBMED_23377541}} | ||
+ | ==Function== | ||
+ | [[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. | ||
==About this Structure== | ==About this Structure== | ||
[[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]. | [[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]. | ||
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:023377541</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] |
Revision as of 08:57, 4 September 2013
Contents |
Crystal structure of Galphaq in complex with full-length human PLCbeta3
Template:ABSTRACT PUBMED 23377541
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.
About this Structure
4gnk is a 5 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
- Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. Full-length Galpha(q)-phospholipase C-beta3 structure reveals interfaces of the C-terminal coiled-coil domain. Nat Struct Mol Biol. 2013 Mar;20(3):355-62. doi: 10.1038/nsmb.2497. Epub 2013 Feb, 3. PMID:23377541 doi:10.1038/nsmb.2497
- ↑ 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
Categories: Homo sapiens | Mus musculus | Phosphoinositide phospholipase C | Lyon, A M. | Tesmer, J J.G. | C2 domain | Calcium binding | Coiled-coil domain | Ef hand | G-protein signaling | Gtp binding | Gtp hydrolysis | Gtp-binding protein alpha subunit | Gtp-binding protein-hydrolase complex | Hydrolase | Lipase | Membrane targeting | Ph domain | Phospholipase | Phospholipase c beta | Phospholipid | Tim barrel domain