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. 1994 May 9;344(1):79-82.
doi: 10.1016/0014-5793(94)00350-5.

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

A Klos  1 , C Mätje, C Rheinheimer, W Bautsch, J Köhl, U Martin, M Burg
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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

A Klos et al. FEBS Lett. .
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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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