1q8m
From Proteopedia
Crystal structure of the human myeloid cell activating receptor TREM-1
Overview
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.
About this Structure
1Q8M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human myeloid cell activating receptor TREM-1., Radaev S, Kattah M, Rostro B, Colonna M, Sun PD, Structure. 2003 Dec;11(12):1527-35. PMID:14656437 Page seeded by OCA on Sat May 3 06:00:05 2008
