SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN

被引：19

作者：

STOCKMAN, BJ ^{[1
]}

SCAHILL, TA ^{[1
]}

STRAKALAITIS, NA ^{[1
]}

BRUNNER, DP ^{[1
]}

YEM, AW ^{[1
]}

DEIBEL, MR ^{[1
]}

机构：

[1] UPJOHN CO, DIV CHEM, KALAMAZOO, MI 49007 USA

来源：

FEBS LETTERS | 1994年 / 349卷 / 01期

关键词：

INTERLEUKIN-1-BETA; INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN; PROTEIN NMR SPECTROSCOPY; ISOTOPIC ENRICHMENT;

D O I：

10.1016/0014-5793(94)00643-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin-1 receptor. In contrast to IL-1 beta, 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-1 beta. By contrast, structurally homologous residues critical for receptor activation are not conserved between the two proteins.

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页码：79 / 83

页数：5

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