8duj

Global map in C1 of RyR1 particles in complex with ImperaCalcin

spinqualitylabelsall models 8duj, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8duj is a 13 chain structure with sequence from Homo sapiens, Oryctolagus cuniculus and Pandinus imperator. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.7Å Ligands: ATP, CA, CFF, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FKB1B_HUMAN Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Publication Abstract from PubMed Calcins are peptides from scorpion venom with the unique ability to cross cell membranes, gaining access to intracellular targets. Ryanodine Receptors (RyR) are intracellular ion channels that control release of Ca(2+) from the endoplasmic and sarcoplasmic reticulum. Calcins target RyRs and induce long-lived subconductance states, whereby single-channel currents are decreased. We used cryo-electron microscopy to reveal the binding and structural effects of imperacalcin, showing that it opens the channel pore and causes large asymmetry throughout the cytosolic assembly of the tetrameric RyR. This also creates multiple extended ion conduction pathways beyond the transmembrane region, resulting in subconductance. Phosphorylation of imperacalcin by protein kinase A prevents its binding to RyR through direct steric hindrance, showing how posttranslational modifications made by the host organism can determine the fate of a natural toxin. The structure provides a direct template for developing calcin analogs that result in full channel block, with potential to treat RyR-related disorders. Cryo-EM analysis of scorpion toxin binding to Ryanodine Receptors reveals subconductance that is abolished by PKA phosphorylation.,Haji-Ghassemi O, Chen YS, Woll K, Gurrola GB, Valdivia CR, Cai W, Li S, Valdivia HH, Van Petegem F Sci Adv. 2023 May 24;9(21):eadf4936. doi: 10.1126/sciadv.adf4936. Epub 2023 May , 24. PMID:37224245 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ryanodine receptor 3D structures

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