CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy
Meng X, Wang G, Viero C, Wang Q, Mi W, Su XD, Wagenknecht T, Williams AJ, Liu Z, Yin CC. CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy. Journal Of Molecular Biology 2009, 387: 320-334. PMID: 19356589, PMCID: PMC2667806, DOI: 10.1016/j.jmb.2009.01.059.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumChloride ChannelsCryoelectron MicroscopyCrystallography, X-RayIon Channel GatingModels, MolecularMuscle, SkeletalProtein BindingProtein ConformationRabbitsRyanodine Receptor Calcium Release ChannelSarcoplasmic ReticulumSurface PropertiesTritiumConceptsCryo-electron microscopyChannel activitySkeletal ryanodine receptorsAffinity of ryanodineSkeletal sarcoplasmic reticulum vesiclesSmall proteinsClamp regionConformational changesPhysiological functionsDomain 5Closed stateSingle-channel recordingsStructural familyRyR1 channelsRyanodine receptorSkeletal muscleRyR1VesiclesOpen probabilityRyR channelsChannel 2Channel recordingsEfflux rateSarcoplasmic reticulum vesiclesReticulum vesicles