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4Z0C

Crystal structure of TLR13-ssRNA13 complex

Summary for 4Z0C
Entry DOI10.2210/pdb4z0c/pdb
DescriptorToll-like receptor 13, DNA (5'-R(P*AP*CP*GP*GP*AP*AP*AP*GP*AP*CP*CP*CP*C)-3'), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsimmune receptor, toll-like receptor, ssrna, immune system
Biological sourceMus musculus (Mouse)
More
Cellular locationEndosome membrane ; Single-pass type I membrane protein : Q6R5N8
Total number of polymer chains4
Total formula weight177966.46
Authors
Song, W.,Han, Z.,Chai, J. (deposition date: 2015-03-26, release date: 2015-10-07, Last modification date: 2024-10-16)
Primary citationSong, W.,Wang, J.,Han, Z.,Zhang, Y.,Zhang, H.,Wang, W.,Chang, J.,Xia, B.,Fan, S.,Zhang, D.,Wang, J.,Wang, H.W.,Chai, J.
Structural basis for specific recognition of single-stranded RNA by Toll-like receptor 13
Nat.Struct.Mol.Biol., 22:782-787, 2015
Cited by
PubMed Abstract: Toll-like receptors (TLRs) have crucial roles in innate immunity, functioning as pattern-recognition receptors. TLR13 recognizes a conserved sequence from bacterial 23S rRNA and then triggers an immune response. Here we report the crystal structure of the mouse TLR13 ectodomain bound by a 13-nt single-stranded (ss) RNA derived from 23S rRNA. The ssRNA induces TLR13 dimerization but assumes a stem-loop-like structure that is completely different from that in the bacterial ribosome but nevertheless is crucial for TLR13 recognition. Most of the RNA nucleotides are splayed out to make base-specific contacts with the concave surface of TLR13, and RNA-specific interactions are important to allow TLR13 to distinguish RNA from DNA. Interestingly, a viral-derived 16-nt ssRNA predicted to form a similar stem-loop-like structure also induces TLR13 activation. Together, our results reveal the structural mechanism of TLR13's sequence- and conformation-specific recognition of ssRNA.
PubMed: 26323037
DOI: 10.1038/nsmb.3080
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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