1fyv: Difference between revisions
New page: left|200px<br /> <applet load="1fyv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fyv, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF... |
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'''CRYSTAL STRUCTURE OF THE TIR DOMAIN OF HUMAN TLR1'''<br /> | '''CRYSTAL STRUCTURE OF THE TIR DOMAIN OF HUMAN TLR1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1FYV 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:// | 1FYV 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=1FYV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: beta-alpha-beta fold parallel beta sheet]] | [[Category: beta-alpha-beta fold parallel beta sheet]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:49:57 2008'' | ||
Revision as of 16:49, 15 February 2008
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CRYSTAL STRUCTURE OF THE TIR DOMAIN OF HUMAN TLR1
OverviewOverview
Toll-like receptors (TLRs) and the interleukin-1 receptor superfamily, (IL-1Rs) are integral to both innate and adaptive immunity for host, defence. These receptors share a conserved cytoplasmic domain, known as, the TIR domain. A single-point mutation in the TIR domain of murine TLR4, (Pro712His, the Lps(d) mutation) abolishes the host immune response to, lipopolysaccharide (LPS), and mutation of the equivalent residue in TLR2, Pro681His, disrupts signal transduction in response to stimulation by, yeast and gram-positive bacteria. Here we report the crystal structures of, the TIR domains of human TLR1 and TLR2 and of the Pro681His mutant of, TLR2. The structures have a large conserved surface patch that also, contains the site of the Lps(d) mutation. Mutagenesis and functional, studies confirm that residues in this surface patch are crucial for, receptor signalling. The Lps(d) mutation does not disturb the structure of, the TIR domain itself. Instead, structural and functional studies indicate, that the conserved surface patch may mediate interactions with the, down-stream MyD88 adapter molecule, and that the Lps(d) mutation may, abolish receptor signalling by disrupting this recruitment.
About this StructureAbout this Structure
1FYV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for signal transduction by the Toll/interleukin-1 receptor domains., Xu Y, Tao X, Shen B, Horng T, Medzhitov R, Manley JL, Tong L, Nature. 2000 Nov 2;408(6808):111-5. PMID:11081518
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