FEBS Letters | |
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 | |
Mätje, C.1  Rheinheimer, C.1  Burg, M.1  Martin, U.1  Bautsch, W.1  Klos, A.1  Köhl, J.1  | |
[1] Institut für Medizinische Mikrobiologie, Medizinische Hochschule Hannover, Konstanty-Gutschowstr. 8, D-30625 Hannover, Germany | |
关键词: C5a; C5a-receptor; Anaphylatoxin; Complement; G-protein; Xenopus; | |
DOI : 10.1016/0014-5793(94)00350-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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