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Crystal structure of the C‐terminal domain of mouse TLR9
Author(s) -
Collins Bernard,
Wilson Ian A.
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24616
Subject(s) - tlr9 , ctd , toll like receptor 9 , receptor , innate immune system , biology , microbiology and biotechnology , architecture domain , immunity , signal transduction , c terminus , dna , immune system , computational biology , genetics , amino acid , gene , computer science , gene expression , oceanography , software architecture , software , enterprise architecture framework , dna methylation , programming language , geology
Toll‐like receptors (TLRs) are important pattern recognition receptors that function in innate immunity. Elucidating the structure and signaling mechanisms of TLR9, a sensor of foreign and endogenous DNA, is essential for understanding its key role in immunity against microbial pathogens as well as in autoimmunity. Abundant evidence suggests that the TLR9‐CTD (C‐terminal domain) by itself is capable of DNA binding and signaling. The crystal structure of unliganded mouse TLR9‐CTD is presented. TLR9‐CTD exhibits one unique feature, a cluster of stacked aromatic and arginine side chains on its concave face. Overall, its structure is most related to the TLR8‐CTD, suggesting a similar mode of ligand binding and signaling. Proteins 2014; 82:2874–2878. © 2014 Wiley Periodicals, Inc.