1q8m
From Proteopedia
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|PDB= 1q8m |SIZE=350|CAPTION= <scene name='initialview01'>1q8m</scene>, resolution 2.6Å | |PDB= 1q8m |SIZE=350|CAPTION= <scene name='initialview01'>1q8m</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= TREM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= TREM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hkf|1HKF]], [[3hfl|3HFL]], [[1tvd|1TVD]], [[1i85|1I85]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8m OCA], [http://www.ebi.ac.uk/pdbsum/1q8m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q8m RCSB]</span> | ||
}} | }} | ||
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[[Category: Rostro, B.]] | [[Category: Rostro, B.]] | ||
[[Category: Sun, P D.]] | [[Category: Sun, P D.]] | ||
| - | [[Category: GSH]] | ||
| - | [[Category: SO4]] | ||
[[Category: immunoglobulin-like]] | [[Category: immunoglobulin-like]] | ||
[[Category: v-type ig-like domain]] | [[Category: v-type ig-like domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:10:15 2008'' |
Revision as of 20:10, 30 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | TREM1 (Homo sapiens) | ||||||
| Related: | 1HKF, 3HFL, 1TVD, 1I85
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the human myeloid cell activating receptor TREM-1
Overview
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.
About this Structure
1Q8M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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