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    Agonist-specific conformational changes in the yeast alpha-factor pheromone receptor

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    Authors
    Bukusoglu, Gul
    Jenness, Duane D.
    UMass Chan Affiliations
    Department of Molecular Genetics and Microbiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1996-09-01
    Keywords
    Amino Acid Sequence; Fungal Proteins; GTP-Binding Proteins; Ligands; Molecular Sequence Data; Peptides; Protein Binding; *Protein Conformation; Receptors, Mating Factor; Receptors, Peptide; *Transcription Factors
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231483/
    Abstract
    The yeast alpha-factor pheromone receptor is a member of the G-protein-coupled receptor family. Limited trypsin digestion of yeast membranes was used to investigate ligand-induced conformational changes in this receptor. The agonist, alpha-factor, accelerated cleavage in the third intracellular loop, whereas the antagonist, desTrp1,Ala3-alpha-factor, reduced the cleavage rate. Thus, the enhanced accessibility of the third intracellular loop is specific to the agonist. alpha-Factor inhibited cleavage weakly at a second site near the cytoplasmic terminus of the seventh transmembrane helix, whereas the antagonist showed a stronger inhibition of cleavage at this site and at another site in the C-terminal domain of the receptor. The alpha-factor-induced conformational changes appeared to be inherent properties of the receptor, as they were retained in G-protein-deficient mutants. Moreover, a mutant receptor (ste2-L236H) that affects the third loop and is defective for G-protein coupling retained the ability to undergo the agonist-induced conformational changes. These results are consistent with a model in which G-protein activation is limited by the availability of specific contacts between the G protein and the third intracellular loop of the receptor. The antagonist appears to promote a distinct conformational state that differs from either the unoccupied or the agonist-occupied state.
    Source

    Mol Cell Biol. 1996 Sep;16(9):4818-23.

    DOI
    10.1128/MCB.16.9.4818
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32958
    PubMed ID
    8756640
    Related Resources

    Link to article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1128/MCB.16.9.4818
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