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Potential ligand-binding residues in rat olfactory receptors identified by correlated mutation analysisA family of G-protein-coupled receptors is believed to mediate the recognition of odor molecules. In order to identify potential ligand-binding residues, we have applied correlated mutation analysis to receptor sequences from the rat. This method identifies pairs of sequence positions where residues remain conserved or mutate in tandem, thereby suggesting structural or functional importance. The analysis supported molecular modeling studies in suggesting several residues in positions that were consistent with ligand-binding function. Two of these positions, dominated by histidine residues, may play important roles in ligand binding and could confer broad specificity to mammalian odor receptors. The presence of positive (overdominant) selection at some of the identified positions provides additional evidence for roles in ligand binding. Higher-order groups of correlated residues were also observed. Each group may interact with an individual ligand determinant, and combinations of these groups may provide a multi-dimensional mechanism for receptor diversity.
Document ID
20050000255
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)
Oliveira, L.
Vriend, G.
Shepherd, G. M.
Date Acquired
August 22, 2013
Publication Date
January 1, 1995
Publication Information
Publication: Receptors & channels
Volume: 3
Issue: 2
ISSN: 1060-6823
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Neuroscience
Non-NASA Center

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