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Amino acids 327–350 of the human C5a‐receptor are not essential for [ 125 I]C5a binding in COS cells and signal transduction in Xenopus oocytes
Author(s) -
Klos A.,
Mätje C.,
Rheinheimer C.,
Bautsch W.,
Köhl J.,
Martin U.,
Burg M.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00350-5
Subject(s) - c5a receptor , xenopus , receptor , mutant , n terminus , amino acid , microbiology and biotechnology , c terminus , biology , peptide sequence , chemistry , biochemistry , complement system , antibody , genetics , gene
The anaphylatoxic peptide C5a is an important inflammatory mediator of the complement system. We have generated human C5a‐receptor (hC5aR) mutants with truncation of its cytosolic carboxyl‐terminus (C‐terminus). Both mutants were analysed for C5a‐binding in transiently expressing COS cells, and one mutant additionally for GTP‐binding regulatory protein (G‐protein) coupling in cRNA‐injected Xenopus oocytes. Our data suggest that (a) amino acids (aa) 314 to 326 as part of the C‐terminus are necessary for proper receptor folding or expression and (b) the receptor C‐terminus distal from position 327 is not critical for receptor expression, folding, binding and G‐protein coupling.