1smo
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(New page: 200px<br /> <applet load="1smo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1smo, resolution 1.47Å" /> '''Crystal Structure o...)
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Revision as of 17:09, 12 November 2007
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Crystal Structure of Human Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) at 1.47 .
Overview
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.
About this Structure
1SMO is a Single protein structure of sequence from Homo sapiens with TLA as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 A., Kelker MS, Foss TR, Peti W, Teyton L, Kelly JW, Wuthrich K, Wilson IA, J Mol Biol. 2004 Sep 24;342(4):1237-48. PMID:15351648
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