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Peptide fragments as models to study the structure of a G‐protein coupled receptor: The α‐factor receptor of Saccharomyces cerevisiae
Author(s) -
Naider Fred,
Arshava Boris,
Ding FaXiang,
Arevalo Enrique,
Becker Jeffrey M.
Publication year - 2001
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2001)60:5<334::aid-bip10175>3.0.co;2-k
Subject(s) - chemistry , g protein coupled receptor , transmembrane domain , peptide , saccharomyces cerevisiae , transmembrane protein , biophysics , receptor , micelle , biochemistry , biology , aqueous solution , organic chemistry , gene
The α‐factor tridecapeptide initiates mating in Saccharomyces cerevisiae upon interaction with Ste2p, its cognate G‐protein coupled receptor (GPCR). This interaction is being used as a paradigm for understanding the structure and mechanism of activation of GPCRs by medium‐sized peptides. In this article, the use of fragments of Ste2p to study its structure is reviewed. Methods of synthesis of peptides corresponding to both extramembranous and transmembrane domains of Ste2p are evaluated and problems that are encountered during synthesis and purification are described. The results from conformational analyses of the peptide fragments using fluorescence spectroscopy, CD, infrared spectroscopy, and NMR spectroscopy in organic‐aqueous mixtures and in the presence of detergent micelles and lipid bilayers are critically reviewed. The data obtained to date provide biophysical evidence for the structure of different domains of Ste2p and indicate that peptides corresponding to these domains have unique biophysical tendencies. The studies carried out on Ste2p fragments indicate that valuable information concerning the structure of the intact receptor can be obtained by studying peptide fragments corresponding to domains of these polytopic integral membrane proteins. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 60: 334–350, 2001