| Literature DB >> 9925780 |
Abstract
Through the high-resolution structure of the gramicidin A channel in lamellar phase lipids and the characterization of specific ion peptide interactions, fundamental principles for ion channel selectivity and conductance efficiency are illustrated with atomic resolution detail. Delocalized cation binding in the first turn of the helix reduces the unfavorable entropy contribution upon binding. Stepwise dehydration minimizes the energy barrier for cation entry and provides valence selectivity in this channel. Three or more water molecules in the monovalent cation binding site result in flexibility in the cation solvation environment causing weak cation size selectivity. Lack of cation induced structural modification avoids the formation of a significant energy barrier, thus permitting efficient cation transport. Copyright 1999 Academic Press.Entities:
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Year: 1999 PMID: 9925780 DOI: 10.1006/jmbi.1998.2434
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469