Potential ligand-binding residues in rat olfactory receptors identified by correlated mutation analysis

Potential ligand-binding residues in rat olfactory receptors identified by correlated mutation analysis

Author Singer, Michael S. Google Scholar
Oliveira, Laerte Autor UNIFESP Google Scholar
Vriend, Gerrit Autor UNIFESP Google Scholar
Shepherd, Gordon M. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
EUROPEAN MOLEC BIOL LAB
Abstract A 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.
Keywords CORRELATED MUTATION
G-PROTEIN-COUPLED RECEPTOR
ODOR RECEPTOR
OLFACTORY RECEPTOR
OVERDOMINANT SELECTION
POSITIVE SELECTION
Language English
Date 1995-01-01
Published in Receptors & Channels. Reading: Harwood Acad Publ Gmbh, v. 3, n. 2, p. 89-95, 1995.
ISSN 1060-6823 (Sherpa/Romeo, impact factor)
Publisher Harwood Acad Publ Gmbh
Extent 89-95
Access rights Closed access
Type Article
Web of Science ID WOS:A1995RZ23500003
URI http://repositorio.unifesp.br/11600/45185

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