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Crystal structure of the human myeloid cell activating receptor TREM-1

机译:人类髓样细胞激活受体TREM-1的晶体结构

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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 Angstrom 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 Angstrom(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 VHVL 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. [References: 45]
机译:髓样细胞(TREM)上表达的触发受体是最近发现的受体家族,它们在先天免疫反应中起重要作用,例如激活炎症反应并响应于微生物介导的感染而导致败血性休克。迄今为止,已经鉴定出人类中的两种TREM受体和小鼠中的几种同源物。我们报告了人类TREM-1胞外域的2.6埃分辨率晶体结构。受体的总体折叠类似于V型免疫球蛋白结构域的折叠,其差异主要位于N末端链上。 TREM-1形成一个具有4100埃(2)界面区域的“头到尾”二聚体,该区域由第一链之间的结构域交换部分介导。这种二聚体形成模式不同于抗体的VHVL结构域或T细胞受体V结构域中存在的“头对头”二聚化。结果,二聚体TREM-1很可能含有两个不同的配体结合位点。 [参考:45]

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