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| | <StructureSection load='1q8m' size='340' side='right'caption='[[1q8m]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1q8m' size='340' side='right'caption='[[1q8m]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1q8m]] is a 4 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=1Q8M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q8M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1q8m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q8M FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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;'>[[1hkf|1hkf]], [[3hfl|3hfl]], [[1tvd|1tvd]], [[1i85|1i85]]</div></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8m OCA], [https://pdbe.org/1q8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q8m RCSB], [https://www.ebi.ac.uk/pdbsum/1q8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8m ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TREM1 ([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=1q8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8m OCA], [http://pdbe.org/1q8m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q8m RCSB], [http://www.ebi.ac.uk/pdbsum/1q8m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Colonna, M]] | + | [[Category: Colonna M]] |
| - | [[Category: Kattah, M]] | + | [[Category: Kattah M]] |
| - | [[Category: Radaev, S]] | + | [[Category: Radaev S]] |
| - | [[Category: Rostro, B]] | + | [[Category: Rostro B]] |
| - | [[Category: Sun, P D]] | + | [[Category: Sun PD]] |
| - | [[Category: Immune system receptor]]
| + | |
| - | [[Category: Immunoglobulin-like]]
| + | |
| - | [[Category: V-type ig-like domain]]
| + | |
| Structural highlights
Function
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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bouchon A, Dietrich J, Colonna M. Cutting edge: inflammatory responses can be triggered by TREM-1, a novel receptor expressed on neutrophils and monocytes. J Immunol. 2000 May 15;164(10):4991-5. PMID:10799849
- ↑ Bouchon A, Facchetti F, Weigand MA, Colonna M. TREM-1 amplifies inflammation and is a crucial mediator of septic shock. Nature. 2001 Apr 26;410(6832):1103-7. PMID:11323674 doi:http://dx.doi.org/10.1038/35074114
- ↑ Radaev S, Kattah M, Rostro B, Colonna M, Sun PD. Crystal structure of the human myeloid cell activating receptor TREM-1. Structure. 2003 Dec;11(12):1527-35. PMID:14656437
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