Although there is a large body of site-directed mutagenesis data that identify the pore-lining sequence of the voltage-gated potassium channel, the structure of this region remains unknown. We have interpreted the available biochemical data as a set of topological and orientational restraints and employed these restraints to produce molecular models of the potassium channel pore region, H5. The H5 sequence has been modeled either as a tetramer of membrane-spanning beta-hairpins, thus producing an eight-stranded beta-barrel, or as a tetramer of incompletely membrane-spanning alpha-helical hairpins, thus producing an eight-staved alpha-helix bundle. In total, restraints-directed modeling has produced 40 different configurations of the beta-ba...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Although there is a large body of site-directed mutagenesis data that identify the pore-lining seque...
Although there is a large body of site-directed mutagenesis data that identify the pore-lining seque...
AbstractA model of the selectivity filter of a voltage-gated K+ (Kv) channel formed by an eight-stra...
AbstractA homology model has been generated for the pore-forming domain of Kir6.2, a component of an...
AbstractA high-resolution crystal structure of KvAP, an archeabacterial voltage-gated potassium (Kv)...
AbstractPotassium channels play fundamental roles in excitable cells. X-ray structures of bacterial ...
AbstractInwardly rectifying potassium channels (Kir), comprising four subunits each with two transme...
AbstractIsolated pore-lining helices derived from three types of K-channel have been analyzed in ter...
AbstractA fundamental question associated with the function of ion channels is the conformational ch...
Recent mutagenesis experiments have confirmed our hypothesis that a segment between S5 and S6 forms ...
AbstractIn the preceding, accompanying article, we present models of the structure and voltage-depen...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Although there is a large body of site-directed mutagenesis data that identify the pore-lining seque...
Although there is a large body of site-directed mutagenesis data that identify the pore-lining seque...
AbstractA model of the selectivity filter of a voltage-gated K+ (Kv) channel formed by an eight-stra...
AbstractA homology model has been generated for the pore-forming domain of Kir6.2, a component of an...
AbstractA high-resolution crystal structure of KvAP, an archeabacterial voltage-gated potassium (Kv)...
AbstractPotassium channels play fundamental roles in excitable cells. X-ray structures of bacterial ...
AbstractInwardly rectifying potassium channels (Kir), comprising four subunits each with two transme...
AbstractIsolated pore-lining helices derived from three types of K-channel have been analyzed in ter...
AbstractA fundamental question associated with the function of ion channels is the conformational ch...
Recent mutagenesis experiments have confirmed our hypothesis that a segment between S5 and S6 forms ...
AbstractIn the preceding, accompanying article, we present models of the structure and voltage-depen...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...
Potassium channels are transmembrane proteins that facilitate the passive and selective flux of K+ i...