1SMO

Crystal Structure of Human Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) at 1.47 .

Summary for 1SMO

• Entry DOI: 10.2210/pdb1smo/pdb
• Related: 1Q8M
• Descriptor: triggering receptor expressed on myeloid cells 1, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: activating receptors, trem-1, innate immune system receptor, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein (Potential). Isoform 2: Secreted (Potential): Q9NP99
• Total number of polymer chains: 2
• Total formula weight: 27663.70

Authors

Kelker, M.S.,Foss, T.R.,Peti, W.,Teyton, L.,Kelly, J.W.,Wilson, I.A. (deposition date: 2004-03-09, release date: 2004-09-21, Last modification date: 2024-10-16)

Primary citation

Kelker, M.S.,Foss, T.R.,Peti, W.,Teyton, L.,Kelly, J.W.,Wilson, I.A.
Crystal Structure of Human Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) at 1.47A.
J.Mol.Biol., 342:1237-1248, 2004

PubMed Abstract: 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-1 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 A 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 1H 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.

PubMed: 15351648
DOI: 10.1016/j.jmb.2004.07.089

Experimental method

X-RAY DIFFRACTION (1.47 Å)