Work

Crystal structure of the C-terminal domain of mouse TLR9

Year: 2014

Type: article

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.

Source: Proteins Structure Function and Bioinformatics

DOI: 10.1002/prot.24616

Authors: Bernard Collins, Ian A. Wilson

Institution: Scripps Research Institute

Language: English

Topic: Immune Response and Inflammation

Subfield: Immunology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of Allergy and Infectious Diseases

Awards: G2269286100, G2563508251, G4940452107, Molecular Basis of Viral Pathogenesis