1o77
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE C713S MUTANT OF THE TIR DOMAIN OF HUMAN TLR2''' | '''CRYSTAL STRUCTURE OF THE C713S MUTANT OF THE TIR DOMAIN OF HUMAN TLR2''' | ||
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Revision as of 00:28, 3 May 2008
CRYSTAL STRUCTURE OF THE C713S MUTANT OF THE TIR DOMAIN OF HUMAN TLR2
Overview
The Toll/interleukin-1 receptor (TIR) domains are conserved modules in the intracellular regions of the Toll-like receptors (TLRs) and interleukin-1 receptors (IL-1Rs). The domains are crucial for the signal transduction by these receptors, through homotypic interactions among the receptor and the downstream adapter TIR domains. Previous studies showed that the BB loop in the structure of the TIR domain forms a prominent conserved feature on the surface and is important for receptor signaling. Here we report the crystal structure of the C713S mutant of the TIR domain of human TLR2. An extensively associated dimer is observed in the crystal structure and mutations of several residues in this dimer interface abolished the function of the receptor. Moreover, the structure shows that the BB loop can adopt different conformations, which are required for the formation of this dimer. This asymmetric dimer might represent the TLR2:TLRx heterodimer in the function of this receptor.
About this Structure
1O77 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
An extensively associated dimer in the structure of the C713S mutant of the TIR domain of human TLR2., Tao X, Xu Y, Zheng Y, Beg AA, Tong L, Biochem Biophys Res Commun. 2002 Nov 29;299(2):216-21. PMID:12437972 Page seeded by OCA on Sat May 3 03:28:08 2008
