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 SO4 and GSH 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 Mon Nov 12 18:51:36 2007
