4QDH

Crystal Structure of the C-terminal Domain of Mouse TLR9

Summary for 4QDH

• Entry DOI: 10.2210/pdb4qdh/pdb
• Descriptor: Variable lymphocyte receptor B, Toll-like receptor 9 chimera, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: glycosylation, immune system
• Biological source: Eptatretus burgeri (Inshore hagfish, mouse); More
• Total number of polymer chains: 2
• Total formula weight: 100529.67

Authors

Collins, B.C.,Wilson, I.A. (deposition date: 2014-05-13, release date: 2014-06-11, Last modification date: 2024-10-30)

Primary citation

Collins, B.,Wilson, I.A.
Crystal structure of the C-terminal domain of mouse TLR9.
Proteins, 82:2874-2878, 2014

PubMed 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.

PubMed: 24888966
DOI: 10.1002/prot.24616

Experimental method

X-RAY DIFFRACTION (2.399 Å)