{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Steele TWE"],"funding":["American Heart Association","NHLBI NIH HHS","National Institutes of Health","NIAMS NIH HHS","Muscular Dystrophy Association"],"pagination":["180-188"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6494473"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["205(2)"],"pubmed_abstract":["Ryanodine receptors (RyRs) are large conductance intracellular channels controlling intracellular calcium homeostasis in myocytes, neurons, and other cell types. Loss of RyR's constitutive cytoplasmic partner FKBP results in channel sensitization, dominant subconductance states, and increased cytoplasmic Ca<sup>2+</sup>. FKBP12 binds to RyR1's cytoplasmic assembly 130 Å away from the ion gate at four equivalent sites in the RyR1 tetramer. To understand how FKBP12 binding alters RyR1's channel properties, we studied the 3D structure of RyR1 alone in the closed conformation in the context of the open and closed conformations of FKBP12-bound RyR1. We analyzed the metrics of conformational changes of existing structures, the structure of the ion gate, and carried out multivariate statistical a"],"journal":["Journal of structural biology"],"pubmed_title":["The FKBP12 subunit modifies the long-range allosterism of the ryanodine receptor."],"pmcid":["PMC6494473"],"funding_grant_id":["MDA352845","R01 AR068431","14GRNT19660003","R56 HL133182"],"pubmed_authors":["Steele TWE","Samso M"],"additional_accession":[]},"is_claimable":false,"name":"The FKBP12 subunit modifies the long-range allosterism of the ryanodine receptor.","description":"Ryanodine receptors (RyRs) are large conductance intracellular channels controlling intracellular calcium homeostasis in myocytes, neurons, and other cell types. Loss of RyR's constitutive cytoplasmic partner FKBP results in channel sensitization, dominant subconductance states, and increased cytoplasmic Ca<sup>2+</sup>. FKBP12 binds to RyR1's cytoplasmic assembly 130 Å away from the ion gate at four equivalent sites in the RyR1 tetramer. To understand how FKBP12 binding alters RyR1's channel properties, we studied the 3D structure of RyR1 alone in the closed conformation in the context of the open and closed conformations of FKBP12-bound RyR1. We analyzed the metrics of conformational changes of existing structures, the structure of the ion gate, and carried out multivariate statistical a","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Feb","modification":"2026-05-07T14:49:41.002Z","creation":"2020-10-30T08:42:47Z"},"accession":"S-EPMC6494473","cross_references":{"pubmed":["30641143"],"doi":["10.1016/j.jsb.2018.12.007"]}}