1fyw

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|PDB= 1fyw |SIZE=350|CAPTION= <scene name='initialview01'>1fyw</scene>, resolution 3.0&Aring;
|PDB= 1fyw |SIZE=350|CAPTION= <scene name='initialview01'>1fyw</scene>, resolution 3.0&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01582 TIR]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyw OCA], [http://www.ebi.ac.uk/pdbsum/1fyw PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1fyw RCSB]</span>
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}}
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:52:37 2008''

Revision as of 03:52, 26 March 2008

Image:1fyw.gif


PDB ID 1fyw

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands: ,
Domains: TIR
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE TIR DOMAIN OF HUMAN TLR2


Contents

Overview

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.

Disease

Known diseases associated with this structure: Colorectal cancer, susceptibility to OMIM:[603028], Leprosy, susceptibility to OMIM:[603028]

About this Structure

1FYW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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