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

Authors: J. P. Simon; Krassimira Angelova; David Puett

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: http://dx.doi.org/10.2174/0929866023408896

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

Publication date: 2002-04-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.