Crystal structure of a voltage-gated K+ channel pore module in a closed state in lipid membranes. J Biol Chem 2012 Dec 14;287(51):43063-70
Date
10/26/2012Pubmed ID
23095758Pubmed Central ID
PMC3522301DOI
10.1074/jbc.M112.415091Scopus ID
2-s2.0-84871124956 (requires institutional sign-in at Scopus site) 23 CitationsAbstract
Voltage-gated K(+) channels underlie the electrical excitability of cells. Each subunit of the functional tetramer consists of the tandem fusion of two modules, an N-terminal voltage-sensor and a C-terminal pore. To investigate how sensor coupling to the pore generates voltage-dependent channel opening, we solved the crystal structure and characterized the function of a voltage-gated K(+) channel pore in a lipid membrane. The structure of a functional channel in a membrane environment at 3.1 Å resolution establishes an unprecedented connection between channel structure and function. The structure is unique in delineating an ion-occupied ready to conduct selectivity filter, a confined aqueous cavity, and a closed activation gate, embodying a dynamic entity trapped in an unstable closed state.
Author List
Santos JS, Asmar-Rovira GA, Han GW, Liu W, Syeda R, Cherezov V, Baker KA, Stevens RC, Montal MAuthor
Wei Liu PhD Professor in the Pharmacology and Toxicology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceConserved Sequence
Crystallography, X-Ray
Ion Channel Gating
Lipid Bilayers
Listeria monocytogenes
Membrane Lipids
Models, Molecular
Molecular Sequence Data
Potassium Channels, Voltage-Gated
Protein Conformation
