6UW9
Cryo-EM structure of the human TRPV3 K169A mutant in the presence of 2-APB, determined in lipid nanodisc
Summary for 6UW9
| Entry DOI | 10.2210/pdb6uw9/pdb |
| EMDB information | 20920 |
| Descriptor | Transient receptor potential cation channel subfamily V member 3 (1 entity in total) |
| Functional Keywords | ion channel trpv3, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 362682.75 |
| Authors | |
| Primary citation | Deng, Z.,Maksaev, G.,Rau, M.,Xie, Z.,Hu, H.,Fitzpatrick, J.A.J.,Yuan, P. Gating of human TRPV3 in a lipid bilayer. Nat.Struct.Mol.Biol., 27:635-644, 2020 Cited by PubMed Abstract: The transient receptor potential cation channel subfamily V member 3 (TRPV3) channel plays a critical role in skin physiology, and mutations in TRPV3 result in the development of a congenital skin disorder, Olmsted syndrome. Here we describe multiple cryo-electron microscopy structures of human TRPV3 reconstituted into lipid nanodiscs, representing distinct functional states during the gating cycle. The ligand-free, closed conformation reveals well-ordered lipids interacting with the channel and two physical constrictions along the ion-conduction pore involving both the extracellular selectivity filter and intracellular helix bundle crossing. Both the selectivity filter and bundle crossing expand upon activation, accompanied by substantial structural rearrangements at the cytoplasmic intersubunit interface. Transition to the inactivated state involves a secondary structure change of the pore-lining helix, which contains a π-helical segment in the closed and open conformations, but becomes entirely α-helical upon inactivation. Together with electrophysiological characterization, structures of TRPV3 in a lipid membrane environment provide unique insights into channel activation and inactivation mechanisms. PubMed: 32572252DOI: 10.1038/s41594-020-0428-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.33 Å) |
Structure validation
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