Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Several ion channel structures have recently been determined, including MthK (a bacterial K+ channel in an open state), KirBac (a bacterial homolog of mammalian inward rectifier K+ channels), KvAP (a bacterial voltage-activated K+ channel) and the pore domain of the nicotinic acetylcholine receptor. Analysis of these structures has increased our understanding of the molecular mechanisms underlying channel gating. A hydrophobic gate appears to operate in a number of channels. Structures of ligand binding domains provide some clues as to how ligand-induced conformational changes control channel gating, but further experimental and computational studies are required before a full picture emerges.

Type

Journal article

Journal

Curr Opin Drug Discov Devel

Publication Date

09/2003

Volume

6

Pages

611 - 619

Keywords

Animals, Bacterial Proteins, Ion Channel Gating, Ion Channels, Ligands, Membrane Proteins, Protein Structure, Quaternary, Protein Structure, Tertiary, Viral Matrix Proteins