5GJV
Structure of the mammalian voltage-gated calcium channel Cav1.1 complex at near atomic resolution
Summary for 5GJV
| Entry DOI | 10.2210/pdb5gjv/pdb |
| EMDB information | 9513 |
| Related PRD ID | PRD_900017 |
| Descriptor | Voltage-dependent L-type calcium channel subunit alpha-1S, 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE, CALCIUM ION, ... (11 entities in total) |
| Functional Keywords | complex, channel, membrane protein |
| Biological source | Oryctolagus cuniculus (Rabbit) More |
| Total number of polymer chains | 5 |
| Total formula weight | 413260.63 |
| Authors | |
| Primary citation | Wu, J.P.,Yan, Z.,Li, Z.Q.,Qian, X.Y.,Lu, S.,Dong, M.Q.,Zhou, Q.,Yan, N. Structure of the voltage-gated calcium channel Cav1.1 at 3.6 angstrom resolution Nature, 537:191-196, 2016 Cited by PubMed Abstract: The voltage-gated calcium (Ca) channels convert membrane electrical signals to intracellular Ca-mediated events. Among the ten subtypes of Ca channel in mammals, Ca1.1 is specified for the excitation-contraction coupling of skeletal muscles. Here we present the cryo-electron microscopy structure of the rabbit Ca1.1 complex at a nominal resolution of 3.6 Å. The inner gate of the ion-conducting α1-subunit is closed and all four voltage-sensing domains adopt an 'up' conformation, suggesting a potentially inactivated state. The extended extracellular loops of the pore domain, which are stabilized by multiple disulfide bonds, form a windowed dome above the selectivity filter. One side of the dome provides the docking site for the α2δ-1-subunit, while the other side may attract cations through its negative surface potential. The intracellular I-II and III-IV linker helices interact with the β-subunit and the carboxy-terminal domain of α1, respectively. Classification of the particles yielded two additional reconstructions that reveal pronounced displacement of β and adjacent elements in α1. The atomic model of the Ca1.1 complex establishes a foundation for mechanistic understanding of excitation-contraction coupling and provides a three-dimensional template for molecular interpretations of the functions and disease mechanisms of Ca and Na channels. PubMed: 27580036DOI: 10.1038/nature19321 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
Download full validation report
