N‐terminal‐methionylated interleukin‐1β has reduced receptor‐binding affinity

FEBS Letters

Wingfield, Paul³  Movva, N.Rao³  Graber, Pierre³  MacDonald, H.Robson²  Gronenborn, Angela M.¹ 

[1] Max-Planck-Institut für Biochemie, 8033 Martinsried, FRG;Ludwig Institute for Cancer Research, Lausanne Branch, 1066 Epalinges, Switzerland;Biogen SA, PO Box 1211, Geneva 14, Switzerland

关键词: Interleukin-1;    Interleukin-1 receptor;    NMR;    Methionine aminopeptidase;    N-terminal processing;   

DOI  :  10.1016/0014-5793(87)80133-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The receptor-binding affinity of recombinant-derived interleukin-1β containing unprocessed N-terminal methionine (MAPV-) was 10-fold lower than protein containing the authentic N-terminal sequence (APV-). Structural analysis of the methionylated and non-methionylated proteins by NMR spectroscopy detected no (or minor) conformational differences. The differences in binding affinity, therefore, suggest that the additional N-terminal methionine causes a small, direct or indirect, perturbation of the receptor-binding region.

【 授权许可】

Unknown