Solution structure of human interleukin‐1 receptor antagonist protein

FEBS Letters

Stockman, Brian J.¹  Strakalaitis, Nancy A.²  Deibel, Martin R.¹  Brunner, David P.²  Yem, Anthony W.¹  Scahill, Terrence A.¹ 

[1] Upjohn Laboratories, The Upjohn Company, 301 Henrietta St., Kalamazoo, MI 49007, USA;Chemical Division, The Upjohn Company, 301 Henrietta St., Kalamazoo, MI 49007, USA

关键词: Interleukin-1β;    Interleukin-1 receptor antagonist protein;    Protein NMR spectroscopy;    Isotopic enrichment;    DQF-COSY;    double quantum filtered correlation spectroscopy;    HMQC;    heteronuclear multiple quantum correlation;    NOE;    nuclear Overhauser enhancement;    IL-1;    interleukin-1;    IRAP;    interleukin-1 receptor antagonist protein;   

DOI  :  10.1016/0014-5793(94)00643-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin-1 receptor. In contrast to IL-1β IRAP binds to the IL-1 receptor but does not elicit a physiological response. We have determined the solution structure of IRAP using NMR spectroscopy. While the overall topology of the two 153-residue proteins is quite similar, functionally critical differences exist concerning the residues of the linear amino acid sequence that constitute structurally homologous regions in the two proteins. Structurally homologous residues important for IL-1 receptor binding are conserved between IRAP and IL-1β. By contrast, structurally homologous residues critical for receptor activation are not conserved between the two proteins.

【 授权许可】

Unknown