6aqf

Crystal structure of A2AAR-BRIL in complex with the antagonist ZM241385 produced from Pichia pastoris

spinqualitylabelsall models 6aqf, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6aqf is a 1 chain structure with sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.51Å Ligands: CLR, OLA, OLB, OLC, ZMA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AA2AR_HUMAN Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.C562_ECOLX Electron-transport protein of unknown function. Publication Abstract from PubMed Signaling across cellular membranes, the 826 human G protein-coupled receptors (GPCRs) govern a wide range of vital physiological processes, making GPCRs prominent drug targets. X-ray crystallography provided GPCR molecular architectures, which also revealed the need for additional structural dynamics data to support drug development. Here, nuclear magnetic resonance (NMR) spectroscopy with the wild-type-like A2A adenosine receptor (A2AAR) in solution provides a comprehensive characterization of signaling-related structural dynamics. All six tryptophan indole and eight glycine backbone (15)N-(1)H NMR signals in A2AAR were individually assigned. These NMR probes provided insight into the role of Asp52(2.50) as an allosteric link between the orthosteric drug binding site and the intracellular signaling surface, revealing strong interactions with the toggle switch Trp 246(6.48), and delineated the structural response to variable efficacy of bound drugs across A2AAR. The present data support GPCR signaling based on dynamic interactions between two semi-independent subdomains connected by an allosteric switch at Asp52(2.50). Allosteric Coupling of Drug Binding and Intracellular Signaling in the A2A Adenosine Receptor.,Eddy MT, Lee MY, Gao ZG, White KL, Didenko T, Horst R, Audet M, Stanczak P, McClary KM, Han GW, Jacobson KA, Stevens RC, Wuthrich K Cell. 2018 Jan 11;172(1-2):68-80.e12. doi: 10.1016/j.cell.2017.12.004. Epub 2017 , Dec 28. PMID:29290469 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adenosine A2A receptor 3D structures

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