4uwe | pdb_00004uwe

Structure of the ryanodine receptor at resolution of 8.5 A in partially open state

spinqualitylabelsall models 4uwe, resolution 8.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uwe is a 4 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: UNK Related: 4uwa Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Muscle contraction is initiated by the release of calcium (Ca2+) from the sarcoplasmic reticulum into the cytoplasm of myocytes through ryanodine receptors (RyRs). RyRs are homotetrameric channels with a molecular mass of more than 2.2 megadaltons that are regulated by several factors, including ions, small molecules and proteins. Numerous mutations in RyRs have been associated with human diseases. The molecular mechanism underlying the complex regulation of RyRs is poorly understood. Using electron cryomicroscopy, here we determine the architecture of rabbit RyR1 at a resolution of 6.1 A. We show that the cytoplasmic moiety of RyR1 contains two large alpha-solenoid domains and several smaller domains, with folds suggestive of participation in protein-protein interactions. The transmembrane domain represents a chimaera of voltage-gated sodium and pH-activated ion channels. We identify the calcium-binding EF-hand domain and show that it functions as a conformational switch allosterically gating the channel. Architecture and conformational switch mechanism of the ryanodine receptor.,Efremov RG, Leitner A, Aebersold R, Raunser S Nature. 2014 Dec 1. doi: 10.1038/nature13916. PMID:25470059 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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