Volume 82, Issue 10 pp. 2874-2878
Structure Note

Crystal structure of the C-terminal domain of mouse TLR9

Bernard Collins

Bernard Collins

Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California

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Ian A. Wilson

Corresponding Author

Ian A. Wilson

Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California

Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California

Correspondence to: Ian A. Wilson; Department of Integrative Structural and Computational Biology, BCC206, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. E-mail: [email protected]Search for more papers by this author
First published: 30 May 2014
Citations: 10

ABSTRACT

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.

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