受体
细胞生物学
免疫受体
先天免疫系统
生物
免疫球蛋白结构域
细胞外
化学
生物化学
作者
Sergei Radaev,Michael Kattah,Bertha Rostro,Marco Colonna,Peter D. Sun
出处
期刊:Structure
[Elsevier]
日期:2003-12-01
卷期号:11 (12): 1527-1535
被引量:62
标识
DOI:10.1016/j.str.2003.11.001
摘要
Triggering receptors expressed on myeloid cells (TREM) are a family of recently discovered receptors that play important roles in innate immune responses, such as to activate inflammatory responses and to contribute to septic shock in response to microbial-mediated infections. To date, two TREM receptors in human and several homologs in mice have been identified. We report the 2.6 A resolution crystal structure of the extracellular domain of human TREM-1. The overall fold of the receptor resembles that of a V-type immunoglobulin domain with differences primarily located in the N-terminal strand. TREM-1 forms a "head-to-tail" dimer with 4100 A(2) interface area that is partially mediated by a domain swapping between the first strands. This mode of dimer formation is different from the "head-to-head" dimerization that existed in V(H)V(L) domains of antibodies or V domains of T cell receptors. As a result, the dimeric TREM-1 most likely contains two distinct ligand binding sites.
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