期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 342, 期 4, 页码 1237-1248出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2004.07.089
关键词
crystal structure; activating receptors; TREM-1; innate immunity; immune system receptor
资金
- NCI NIH HHS [CA58896] Funding Source: Medline
- NIAID NIH HHS [T32 AI077606, AI42266] Funding Source: Medline
The triggering receptor expressed on myeloid cells (TREM) family of single extracellular immunoglobulin receptors includes both activating and inhibitory isoforms whose ligands are unknown. TREM-1 activation amplifies the Toll-like receptor initiated responses to invading pathogens allowing the secretion of pro-inflammatory chemokines and cytokines. Hence, TREM-I amplifies the inflammation induced by both bacteria and fungi, and thus represents a potential therapeutic target. We report the crystal structure of the human TREM-1 extracellular domain at 1.47 Angstrom resolution. The overall fold places it within the V-type immunoglobulin domain family and reveals close homology with Ig domains from antibodies, T-cell receptors and other activating receptors, such as NKp44. With the additional use of analytical ultracentrifugation and H-1 NMR spectroscopy of both human and mouse TREM-1, we have conclusively demonstrated the monomeric state of this extracellular ectodomain in solution and, presumably, of the TREM family in general. (C) 2004 Elsevier Ltd. All rights reserved.
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