1smo

<table><tr><td colspan='2'>[[1smo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SMO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q8m|1q8m]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trem-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1smo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smo OCA], [http://pdbe.org/1smo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1smo RCSB], [http://www.ebi.ac.uk/pdbsum/1smo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1smo ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TREM1_HUMAN TREM1_HUMAN]] Stimulates neutrophil and monocyte-mediated inflammatory responses. Triggers release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a crucial mediator of septic shock.<ref>PMID:10799849</ref> <ref>PMID:11323674</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:15351648</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1smo" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Foss, T R]]

[[Category: Kelker, M S]]

[[Category: Kelly, J W]]

[[Category: Peti, W]]

[[Category: Teyton, L]]

[[Category: Wilson, I A]]

[[Category: Trem-1]]