6J8E
Human Nav1.2-beta2-KIIIA ternary complex
Summary for 6J8E
| Entry DOI | 10.2210/pdb6j8e/pdb |
| EMDB information | 9780 |
| Descriptor | Sodium channel subunit beta-2, Sodium channel protein type 2 subunit alpha, Mu-conotoxin KIIIA, ... (8 entities in total) |
| Functional Keywords | transmembrane protein, membrane protein, membrane protein-toxin complex, membrane protein/toxin |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 251187.00 |
| Authors | |
| Primary citation | Pan, X.,Li, Z.,Huang, X.,Huang, G.,Gao, S.,Shen, H.,Liu, L.,Lei, J.,Yan, N. Molecular basis for pore blockade of human Na+channel Nav1.2 by the mu-conotoxin KIIIA. Science, 363:1309-1313, 2019 Cited by PubMed Abstract: The voltage-gated sodium channel Na1.2 is responsible for the initiation and propagation of action potentials in the central nervous system. We report the cryo-electron microscopy structure of human Na1.2 bound to a peptidic pore blocker, the μ-conotoxin KIIIA, in the presence of an auxiliary subunit, β2, to an overall resolution of 3.0 angstroms. The immunoglobulin domain of β2 interacts with the shoulder of the pore domain through a disulfide bond. The 16-residue KIIIA interacts with the extracellular segments in repeats I to III, placing Lys at the entrance to the selectivity filter. Many interacting residues are specific to Na1.2, revealing a molecular basis for KIIIA specificity. The structure establishes a framework for the rational design of subtype-specific blockers for Na channels. PubMed: 30765605DOI: 10.1126/science.aaw2999 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
Download full validation report
