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Positive selection moments identify potential functional residues in human olfactory receptorsCorrelated mutation analysis and molecular models of olfactory receptors have provided evidence that residues in the transmembrane domains form a binding pocket for odor ligands. As an independent test of these results, we have calculated positive selection moments for the alpha-helical sixth transmembrane domain (TM6) of human olfactory receptors. The moments can be used to identify residues that have been preferentially affected by positive selection and are thus likely to interact with odor ligands. The results suggest that residue 622, which is commonly a serine or threonine, could form critical H-bonds. In some receptors a dual-serine subsite, formed by residues 622 and 625, could bind hydroxyl determinants on odor ligands. The potential importance of these residues is further supported by site-directed mutagenesis in the beta-adrenergic receptor. The findings should be of practical value for future physiological studies, binding assays, and site-directed mutagenesis.
Document ID
20040173294
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Singer, M. S.
(Yale University School of Medicine New Haven, CT 06510, United States)
Weisinger-Lewin, Y.
Lancet, D.
Shepherd, G. M.
Date Acquired
August 22, 2013
Publication Date
January 1, 1996
Publication Information
Publication: Receptors & channels
Volume: 4
Issue: 3
ISSN: 1060-6823
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Discipline Neuroscience

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