Comparative modeling studies of rat amiloride-sensitive cation channel 1, neuronal isoform b

Abstract

Acid-sensing ion channels (ASICs) of the epithelial sodium channel/degenerin (ENaC/DEG) gene family are protongated cation channels. ASICs have two transmembrane segments which are hydrophobic. Various proton-gated ion channels suggest that, ASIC and MDEG probably seems to be the first two members of this family and the genes for the new channels remain to be discovered. The presence of a large extracellular domain between two transmembrane alpha-helices and the short NH2 and COOH terminal cytoplasmic segments, characterizes these proteins. In order to relate the three-dimensional (3D) structure to their physiological function, channel proteins have been the focus of various computational approaches. On the basis of available X-ray structures, structural models of channels may be constructed by homology modeling. Here we present 3D structure of rat Amiloride-sensitive cation channel 1, neuronal isoform B through Comparative Modeling studies. Our studies will be useful in understanding the biochemical functions and interaction properties in detail.