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

Authors: J. P. Simon¹; Krassimira Angelova¹; David Puett¹

Source: Protein and Peptide Letters, Volume 9, Number 2, April 2002 , pp. 153-158(6)

Publisher: Bentham Science Publishers

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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.

Keywords: transmembrane helices; lutropin receptor; ab initio calculation

Document Type: Review article

DOI: 10.2174/0929866023408896

Affiliations: 1: Department of Biochemistry & Molecular Biology, University of Georgia, Athens, GA 30602, USA

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