4ib4

Crystal structure of the chimeric protein of 5-HT2B-BRIL in complex with ergotamine

spinqualitylabelsall models 4ib4, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ib4 is a 1 chain structure with sequence from Escherichia coli and Homo sapiens. The August 2013 RCSB PDB Molecule of the Month feature on Serotonin Receptor by David Goodsell is 10.2210/rcsb_pdb/mom_2013_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: CLR, ERM, OLA, OLB, OLC, PEG, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C562_ECOLX Electron-transport protein of unknown function.5HT2B_HUMAN This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Plays a role in the regulation of impulsive behavior. Publication Abstract from PubMed Drugs active at G protein-coupled receptors (GPCRs) can differentially modulate either canonical or noncanonical signaling pathways via a phenomenon known as functional selectivity or biased signaling. We report biochemical studies that show that the hallucinogen lysergic acid diethylamide (LSD), its precursor ergotamine (ERG), and related ergolines display strong functional selectivity for beta-arrestin signaling at the 5-hydroxytryptamine (5-HT) receptor 5-HT2B, while being relatively unbiased at the 5-HT1B receptor. To investigate the structural basis for biased signaling, we determined the crystal structure of the human 5-HT2B receptor bound to ERG, and compared it with the 5-HT1B/ERG structure. Given the relatively poor understanding of GPCR structure-function to date, insight into different GPCR signaling pathways is important to better understand both adverse and favorable therapeutic activities. Structural Features for Functional Selectivity at Serotonin Receptors.,Wacker D, Wang C, Katritch V, Han GW, Huang XP, Vardy E, McCorvy JD, Jiang Y, Chu M, Siu FY, Liu W, Xu HE, Cherezov V, Roth BL, Stevens RC Science. 2013 Mar 21. PMID:23519215 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 5-hydroxytryptamine receptor 3D structures

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