Molecular Modeling of Transmembrane Helices 6 and 7 of the Heptahelical Lutropin Receptor
In response to ligand binding and activating mutations, the lutropin receptor undergoes a conformational change to trigger a cellular response. D556 is the most common locus for naturally occurring activating mutations of the lutropin receptor, and a D556A mutant is shown to be constitutively active. A water-mediated proton transfer is postulated as part of the transmembrane signaling mechanism. Using energy minimization and ab initio calculations, a hydrogen bonding network involving a highly constrained water molecule(s) and D556 (helix 6) and N593 / N597 / Y601 (helix 7) is presented.
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Document Type: Review Article
Affiliations: Department of Biochemistry & Molecular Biology, University of Georgia, Athens, GA 30602, USA
Publication date: 2002-04-01
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