1Q8M

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

1Q8M の概要

• エントリーDOI: 10.2210/pdb1q8m/pdb
• 関連するPDBエントリー: 1HKF 1I85 1TVD 3HFL
• 分子名称: triggering receptor expressed on myeloid cells 1, SULFATE ION, GLUTATHIONE, ... (4 entities in total)
• 機能のキーワード: v-type ig-like domain, immunoglobulin-like, immune system receptor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Cell membrane; Single-pass type I membrane protein (Potential). Isoform 2: Secreted (Potential): Q9NP99
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61076.60

構造登録者

Radaev, S.,Kattah, M.,Rostro, B.,Colonna, M.,Sun, P.D. (登録日: 2003-08-21, 公開日: 2003-12-09, 最終更新日: 2022-12-21)

主引用文献

Radaev, S.,Kattah, M.,Rostro, B.,Colonna, M.,Sun, P.D.
Crystal structure of the human myeloid cell activating receptor TREM-1
Structure, 11:1527-1535, 2003

PubMed Abstract: 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.

PubMed: 14656437
DOI: 10.1016/j.str.2003.11.001

実験手法

X-RAY DIFFRACTION (2.6 Å)