1q8m
From Proteopedia
(New page: 200px<br /> <applet load="1q8m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q8m, resolution 2.6Å" /> '''Crystal structure of...) |
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- | [[Image:1q8m. | + | [[Image:1q8m.jpg|left|200px]]<br /><applet load="1q8m" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1q8m, resolution 2.6Å" /> | caption="1q8m, resolution 2.6Å" /> | ||
'''Crystal structure of the human myeloid cell activating receptor TREM-1'''<br /> | '''Crystal structure of the human myeloid cell activating receptor TREM-1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 1Q8M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and GSH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Q8M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: v-type ig-like domain]] | [[Category: v-type ig-like domain]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:43:02 2008'' |
Revision as of 14:43, 15 February 2008
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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 with and as ligands. 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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