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 1.47&Aring;" /> '''Crystal Structure o...)
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'''Crystal Structure of Human Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) at 1.47 .'''<br />
'''Crystal Structure of Human Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) at 1.47 .'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1SMO 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 TLA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SMO OCA].
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1SMO 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=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMO OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Foss, T.R.]]
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[[Category: Foss, T R.]]
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[[Category: Kelker, M.S.]]
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[[Category: Kelker, M S.]]
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[[Category: Kelly, J.W.]]
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[[Category: Kelly, J W.]]
[[Category: Peti, W.]]
[[Category: Peti, W.]]
[[Category: Teyton, L.]]
[[Category: Teyton, L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: TLA]]
[[Category: TLA]]
[[Category: activating receptors]]
[[Category: activating receptors]]
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[[Category: trem-1]]
[[Category: trem-1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:15:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:07 2008''

Revision as of 13:03, 21 February 2008


1smo, resolution 1.47Å

Drag the structure with the mouse to rotate

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 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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