1byw
From Proteopedia
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STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL
Contents |
Overview
The HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability, and when defective, it underlies one form of the long QT syndrome. We have determined the crystal structure of the HERG K+ channel N-terminal domain and studied its role as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it tightly binds. The presence of the domain attached to the channel slows the rate of deactivation. Given the roles of PAS domains in biology, we propose that the HERG N-terminal domain has a regulatory function.
Disease
Known diseases associated with this structure: Lathosterolosis OMIM:[602286], Long QT syndrome, acquired, susceptibility to OMIM:[152427], Long QT syndrome-2 OMIM:[152427], Short QT syndrome-1 OMIM:[152427]
About this Structure
1BYW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain., Morais Cabral JH, Lee A, Cohen SL, Chait BT, Li M, Mackinnon R, Cell. 1998 Nov 25;95(5):649-55. PMID:9845367
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