5X0M
Structure of a eukaryotic voltage-gated sodium channel at near atomic resolution
Summary for 5X0M
| Entry DOI | 10.2210/pdb5x0m/pdb |
| EMDB information | 6698 |
| Descriptor | Sodium channel protein, beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | ion channel, membrane protein |
| Biological source | Periplaneta americana (American cockroach) |
| Total number of polymer chains | 1 |
| Total formula weight | 187778.02 |
| Authors | |
| Primary citation | Shen, H.,Zhou, Q.,Pan, X.,Li, Z.,Wu, J.,Yan, N. Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution. Science, 355:-, 2017 Cited by PubMed Abstract: Voltage-gated sodium (Na) channels are responsible for the initiation and propagation of action potentials. They are associated with a variety of channelopathies and are targeted by multiple pharmaceutical drugs and natural toxins. Here, we report the cryogenic electron microscopy structure of a putative Na channel from American cockroach (designated NaPaS) at 3.8 angstrom resolution. The voltage-sensing domains (VSDs) of the four repeats exhibit distinct conformations. The entrance to the asymmetric selectivity filter vestibule is guarded by heavily glycosylated and disulfide bond-stabilized extracellular loops. On the cytoplasmic side, a conserved amino-terminal domain is placed below VSD, and a carboxy-terminal domain binds to the III-IV linker. The structure of NaPaS establishes an important foundation for understanding function and disease mechanism of Na and related voltage-gated calcium channels. PubMed: 28183995DOI: 10.1126/science.aal4326 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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