4gnk

Crystal structure of Galphaq in complex with full-length human PLCbeta3Crystal structure of Galphaq in complex with full-length human PLCbeta3

Structural highlights 4gnk is a 5 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , Gene: g alpha q, Gnaq (Mus musculus), phospholipase c beta 3, PLCB3 (Homo sapiens) Activity: Phosphoinositide phospholipase C, with EC number 3.1.4.11 Resources: FirstGlance, OCA, RCSB, PDBsum 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). [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) 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Guanine nucleotide-binding protein

spinqualitylabelsall models 4gnk, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image