Amino acids 327-350 of the human C5a-receptor are not essential for [125I]C5a binding in COS cells and signal transduction in Xenopus oocytes.
FEBS Lett
; 344(1): 79-82, 1994 May 09.
Article
em En
| MEDLINE
| ID: mdl-8181569
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oócitos
/
Fragmentos de Peptídeos
/
Receptores de Complemento
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Transdução de Sinais
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Complemento C5a
Limite:
Animals
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Female
/
Humans
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article