Structure of the activating IL-1 receptor signaling complex

被引：98

作者：

Thomas, Christoph ^{[1
,2
,3
]}

Bazan, J. Fernando ^{[4
]}

Garcia, K. Christopher ^{[1
,2
,3
]}

机构：

[1] Stanford Univ, Howard Hughes Med Inst, Sch Med, Stanford, CA 94305 USA

[2] Stanford Univ, Sch Med, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA

[3] Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA

[4] NeuroScience Inc, Osceola, WI USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 04期

关键词：

CRYSTAL-STRUCTURE; FAMILY; CYTOKINES; HEPARIN; REVEALS; BINDING; BETA;

D O I：

10.1038/nsmb.2260

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 (IL-1)-family cytokines are mediators of innate and adaptive immunity. They exert proinflammatory effects by binding a primary receptor that recruits a receptor accessory protein to form a signaling-competent heterotrimeric complex. Here we present the crystal structure of IL-1 beta bound to its primary receptor IL-1RI and its receptor accessory protein IL-1RAcP, providing insight into how IL-1-type cytokines initiate signaling and revealing an evolutionary relationship with the fibroblast growth factor receptor family.

引用

页码：455 / 457

页数：3

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