Summary for 6JRR
| Entry DOI | 10.2210/pdb6jrr/pdb |
| EMDB information | 9879 |
| Descriptor | RyR2, Peptidyl-prolyl cis-trans isomerase FKBP1B, ZINC ION, ... (6 entities in total) |
| Functional Keywords | cryo-em, membrane protein, membrane protein-isomerase complex, membrane protein/isomerase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 2310043.94 |
| Authors | Gong, D.S.,Chi, X.M.,Zhou, G.W.,Huang, G.X.Y.,Lei, J.L.,Yan, N. (deposition date: 2019-04-05, release date: 2019-07-17, Last modification date: 2024-03-27) |
| Primary citation | Gong, D.,Chi, X.,Wei, J.,Zhou, G.,Huang, G.,Zhang, L.,Wang, R.,Lei, J.,Chen, S.R.W.,Yan, N. Modulation of cardiac ryanodine receptor 2 by calmodulin. Nature, 572:347-351, 2019 Cited by PubMed Abstract: The high-conductance intracellular calcium (Ca) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca-dependent manner. Here we reveal the regulatory mechanism by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under eight conditions. Apo-CaM and Ca-CaM bind to distinct but overlapping sites in an elongated cleft formed by the handle, helical and central domains. The shift in CaM-binding sites on RyR2 is controlled by Ca binding to CaM, rather than to RyR2. Ca-CaM induces rotations and intradomain shifts of individual central domains, resulting in pore closure of the PCB95 and Ca-activated channel. By contrast, the pore of the ATP, caffeine and Ca-activated channel remains open in the presence of Ca-CaM, which suggests that Ca-CaM is one of the many competing modulators of RyR2 gating. PubMed: 31278385DOI: 10.1038/s41586-019-1377-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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