1O77

CRYSTAL STRUCTURE OF THE C713S MUTANT OF THE TIR DOMAIN OF HUMAN TLR2

Summary for 1O77

• Entry DOI: 10.2210/pdb1o77/pdb
• Related: 1FYW
• Descriptor: TOLL-LIKE RECEPTOR 2 (1 entity in total)
• Functional Keywords: immune system/membrane protein, known biological activity receptor, immune response, inflammatory response, transmembrane, leucine-rich repeat, glycoprotein, 3d-structure., immune system-membrane protein complex
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Membrane; Single-pass type I membrane protein (By similarity): O60603
• Total number of polymer chains: 5
• Total formula weight: 87620.71

Authors

Tao, X.,Xu, Y.,Ye, Z.,Beg, A.A.,Tong, L. (deposition date: 2002-10-24, release date: 2002-11-21, Last modification date: 2024-10-16)

Primary citation

Tao, X.,Xu, Y.,Zheng, Y.,Beg, A.A.,Tong, L.
An Extensively Associated Dimer in the Structure of the C713S Mutant of the Tir Domain of Human Tlr2
Biochem.Biophys.Res.Commun., 299:216-, 2002

PubMed Abstract: 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.

PubMed: 12437972
DOI: 10.1016/S0006-291X(02)02581-0

Experimental method

X-RAY DIFFRACTION (3.2 Å)