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.

Molecular modelling studies of the transmembrane domain, and in particular of the pore-forming region, of voltage-gated K+channels are reviewed. Sequence analysis methods are used to define transmembrane helices and their orientation within the intact channel protein. A detailed comparison is presented of three models (from different research groups) of the (H5)4domain. These models have all been generated by systematic attempts to fit experimental data which identify pore-lining sidechains. The models are analysed in terms of pore radius profiles and predicted conductances, as well as the extent of their agreement with published mutagenesis data. An extended pore domain model, (S5-H5-S6)4, which includes the S5 and S6 helices packed around a bulged β-barrel of (H5)4, is also described and analysed.

Original publication




Journal article


Perspectives in Drug Discovery and Design

Publication Date





187 - 214