1q8m
From Proteopedia
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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 with and as ligands. 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 Fri Feb 15 16:43:02 2008
