8j97

Structure of Muscarinic receptor (M2R) in complex with beta-arrestin1 (Local refine, cross-linked)

spinqualitylabelsall models 8j97, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8j97 is a 4 chain structure with sequence from Bos taurus, Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Ligands: SEP, TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed beta-arrestins (betaarrs) are multifunctional proteins involved in signaling and regulation of seven transmembrane receptors (7TMRs), and their interaction is driven primarily by agonist-induced receptor activation and phosphorylation. Here, we present seven cryo-electron microscopy structures of betaarrs either in the basal state, activated by the muscarinic receptor subtype 2 (M2R) through its third intracellular loop, or activated by the betaarr-biased decoy D6 receptor (D6R). Combined with biochemical, cellular, and biophysical experiments, these structural snapshots allow the visualization of atypical engagement of betaarrs with 7TMRs and also reveal a structural transition in the carboxyl terminus of betaarr2 from a beta strand to an alpha helix upon activation by D6R. Our study provides previously unanticipated molecular insights into the structural and functional diversity encoded in 7TMR-betaarr complexes with direct implications for exploring novel therapeutic avenues. Molecular insights into atypical modes of beta-arrestin interaction with seven transmembrane receptors.,Maharana J, Sano FK, Sarma P, Yadav MK, Duan L, Stepniewski TM, Chaturvedi M, Ranjan A, Singh V, Saha S, Mahajan G, Chami M, Shihoya W, Selent J, Chung KY, Banerjee R, Nureki O, Shukla AK Science. 2024 Jan 5;383(6678):101-108. doi: 10.1126/science.adj3347. Epub 2024 , Jan 4. PMID:38175886 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA