Molecular Modeling of Transmembrane Helices 6 and 7 of the Heptahelical Lutropin Receptor

Title: Molecular Modeling of Transmembrane Helices 6 and 7 of the Heptahelical Lutropin Receptor

Volume: 9 Issue: 2

Author(s): J. Paul Simon, Krassimira Angelova and David Puett

Affiliation:

Keywords: transmembrane helices, lutropin receptor, ab initio calculation

Abstract: 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.

Cite this article as:

Simon Paul J., Angelova Krassimira and Puett David, Molecular Modeling of Transmembrane Helices 6 and 7 of the Heptahelical Lutropin Receptor, Protein & Peptide Letters 2002; 9 (2) . https://dx.doi.org/10.2174/0929866023408896

DOI https://dx.doi.org/10.2174/0929866023408896	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305