2frg
From Proteopedia
(New page: 200px<br /> <applet load="2frg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2frg, resolution 1.19Å" /> '''Structure of the im...) |
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| - | [[Image:2frg.gif|left|200px]]<br /> | + | [[Image:2frg.gif|left|200px]]<br /><applet load="2frg" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2frg" size=" | + | |
caption="2frg, resolution 1.19Å" /> | caption="2frg, resolution 1.19Å" /> | ||
'''Structure of the immunoglobulin-like domain of human TLT-1'''<br /> | '''Structure of the immunoglobulin-like domain of human TLT-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Triggering receptor expressed on myeloid cells like transcript-1 (TLT-1) | + | Triggering receptor expressed on myeloid cells like transcript-1 (TLT-1) is an abundant platelet-specific, type I transmembrane receptor. The extracellular fragment of TLT-1 consists of a single, immunoglobulin-like domain connected to the platelet cell membrane by a linker region called the stalk. Here we present evidence that a soluble fragment of the TLT-1 extracellular domain is found in serum of humans and mice and that an isoform of similar mass is released from platelets following activation with thrombin. We also report the crystal structure of the immunoglobulin domain of TLT-1 determined at the resolution of 1.19 A. The structure of TLT-1 is similar to other immunoglobulin-like variable domains, particularly those of triggering receptor expressed on myeloid cells-1 (TREM-1), the natural killer cell-activating receptor NKp44, and the polymeric immunoglobulin receptor. Particularly interesting is a 17-amino acid segment of TLT-1, homologous to a fragment of murine TREM-1, which, in turn, showed activity in blocking the TREM-1-mediated inflammatory responses in mice. Structural similarity to TREM-1 and polymeric immunoglobulin receptor, and evidence for a naturally occurring soluble fragment of the TLT-1 extracellular domain, suggest that this immunoglobulin-like domain autonomously plays an as yet unidentified, functional role. |
==About this Structure== | ==About this Structure== | ||
| - | 2FRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2FRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FRG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gattis, J | + | [[Category: Gattis, J L.]] |
[[Category: Lubkowski, J.]] | [[Category: Lubkowski, J.]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
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[[Category: triggering receptor]] | [[Category: triggering receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:22 2008'' |
Revision as of 15:24, 21 February 2008
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Structure of the immunoglobulin-like domain of human TLT-1
Overview
Triggering receptor expressed on myeloid cells like transcript-1 (TLT-1) is an abundant platelet-specific, type I transmembrane receptor. The extracellular fragment of TLT-1 consists of a single, immunoglobulin-like domain connected to the platelet cell membrane by a linker region called the stalk. Here we present evidence that a soluble fragment of the TLT-1 extracellular domain is found in serum of humans and mice and that an isoform of similar mass is released from platelets following activation with thrombin. We also report the crystal structure of the immunoglobulin domain of TLT-1 determined at the resolution of 1.19 A. The structure of TLT-1 is similar to other immunoglobulin-like variable domains, particularly those of triggering receptor expressed on myeloid cells-1 (TREM-1), the natural killer cell-activating receptor NKp44, and the polymeric immunoglobulin receptor. Particularly interesting is a 17-amino acid segment of TLT-1, homologous to a fragment of murine TREM-1, which, in turn, showed activity in blocking the TREM-1-mediated inflammatory responses in mice. Structural similarity to TREM-1 and polymeric immunoglobulin receptor, and evidence for a naturally occurring soluble fragment of the TLT-1 extracellular domain, suggest that this immunoglobulin-like domain autonomously plays an as yet unidentified, functional role.
About this Structure
2FRG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the extracellular domain of triggering receptor expressed on myeloid cells like transcript-1 and evidence for a naturally occurring soluble fragment., Gattis JL, Washington AV, Chisholm MM, Quigley L, Szyk A, McVicar DW, Lubkowski J, J Biol Chem. 2006 May 12;281(19):13396-403. Epub 2006 Feb 27. PMID:16505478
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