6CNN
Cryo-EM structure of the human SK4/calmodulin channel complex in the Ca2+ bound state I
Summary for 6CNN
| Entry DOI | 10.2210/pdb6cnn/pdb |
| EMDB information | 7537 7538 7539 |
| Descriptor | Intermediate conductance calcium-activated potassium channel protein 4, Calmodulin-1, POTASSIUM ION, ... (6 entities in total) |
| Functional Keywords | ion channel, neuroscience, calmodulin, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 266206.72 |
| Authors | Lee, C.H.,MacKinnon, R. (deposition date: 2018-03-08, release date: 2018-05-02, Last modification date: 2024-03-13) |
| Primary citation | Lee, C.H.,MacKinnon, R. Activation mechanism of a human SK-calmodulin channel complex elucidated by cryo-EM structures. Science, 360:508-513, 2018 Cited by PubMed Abstract: Small-conductance Ca-activated K (SK) channels mediate neuron excitability and are associated with synaptic transmission and plasticity. They also regulate immune responses and the size of blood cells. Activation of SK channels requires calmodulin (CaM), but how CaM binds and opens SK channels has been unclear. Here we report cryo-electron microscopy (cryo-EM) structures of a human SK4-CaM channel complex in closed and activated states at 3.4- and 3.5-angstrom resolution, respectively. Four CaM molecules bind to one channel tetramer. Each lobe of CaM serves a distinct function: The C-lobe binds to the channel constitutively, whereas the N-lobe interacts with the S4-S5 linker in a Ca-dependent manner. The S4-S5 linker, which contains two distinct helices, undergoes conformational changes upon CaM binding to open the channel pore. These structures reveal the gating mechanism of SK channels and provide a basis for understanding SK channel pharmacology. PubMed: 29724949DOI: 10.1126/science.aas9466 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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