A computational model of the HBK2 potassium channel ion pore.
A computational model of the putative ion pore region of the HBK2 potassium channel was developed. Utilizing experimentally derived constraints, conformations corresponding to both the open and closed states of the ion pore were determined. Also, a conformational basis for the different sensitivites of the internal and external tetraethylammonium binding sites has been proposed. The model presented here suggests a role for other regions of the HBK2 protein in determining the ion pore conformation.
Jin
A Y
AY
Department of Chemistry, Queen's University, Kingston, Ontario, Canada.
Weaver
D F
DF
D000595:Amino Acid Sequence; D003198:Computer Simulation; D051667:Kv1.6 Potassium Channel; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015221:Potassium Channels / Q000737:chemistry*; D024642:Potassium Channels, Voltage-Gated; D011487:Protein Conformation; D051637:Shaker Superfamily of Potassium Channels; D019789:Tetraethylammonium; D013757:Tetraethylammonium Compounds / Q000737:chemistry
C064389:KCNA6 protein, human; D051667:Kv1.6 Potassium Channel; D008565:Membrane Proteins; D015221:Potassium Channels; D024642:Potassium Channels, Voltage-Gated; D051637:Shaker Superfamily of Potassium Channels; D013757:Tetraethylammonium Compounds; D019789:Tetraethylammonium