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Domains of the human neutrophil N-formyl peptide receptor involved in G protein coupling. Mapping with receptor-derived peptides

Academic Article
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Overview

authors

  • Schreiber, R. E.
  • Prossnitz, E. R.
  • Ye, R. D.
  • Cochrane, Charles
  • Bokoch, G. M.

publication date

  • January 1994

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Chemotactic signaling by the human neutrophil N-formyl peptide receptor requires its association with heterotrimeric G protein. Synthetic peptides and a fusion protein derived from the intracellular regions of the receptor were used to identify sites which interact with G protein. A peptide derived from the second intracellular loop (C12R), and peptides (F15R and S22L) and a fusion protein derived from the receptor's carboxyl terminus inhibited binding of anti-Gi alpha antibody (R16,17) to Gi alpha in a competitive enzyme-linked immunoassay, and antagonized pertussis-toxin catalyzed ADP-ribosylation of Gi alpha. C12R also inhibited G protein-dependent, high affinity ligand binding to the receptor and physical coupling of receptor to G protein. In contrast, a peptide consisting of the entire third loop of the N-formyl peptide receptor was totally inactive in these assays. Collectively, these data suggest that the second intracellular loop and the carboxyl-terminal tail are important for effective N-formyl peptide receptor/G protein coupling, but that the third intracellular loop is less important in coupling, unlike previous findings with other G protein-coupled receptor systems. The chemoattractant receptor family may rely on different structural determinants to interact with GTP-binding proteins.

subject areas

  • Amino Acid Sequence
  • Binding Sites
  • GTP-Binding Proteins
  • Humans
  • In Vitro Techniques
  • Molecular Sequence Data
  • N-Formylmethionine Leucyl-Phenylalanine
  • Neutrophils
  • Peptides
  • Receptors, Formyl Peptide
  • Receptors, Immunologic
  • Receptors, Peptide
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 8276814
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Additional Document Info

start page

  • 326

end page

  • 331

volume

  • 269

issue

  • 1

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