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PDBsum entry 4oi8

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protein dna_rna Protein-protein interface(s) links
Transport protein,signaling protein/DNA PDB id
4oi8

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
211 a.a.
DNA/RNA
Waters ×25
PDB id:
4oi8
Name: Transport protein,signaling protein/DNA
Title: Rage is a nucleic acid receptor that promotes inflammatory responses to DNA.
Structure: Advanced glycosylation end product-specific receptor. Chain: a, b. Fragment: unp residues 23-237. Synonym: rage, receptor for advanced glycosylation end products. Engineered: yes. 5'-d( Cp Cp Ap Tp Gp Ap Cp Tp Gp Tp Ap Gp Gp Ap Ap Ap Cp Tp Cp Tp Ap Gp A)-3'. Chain: e. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ager, rage. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic: yes
Resolution:
3.10Å     R-factor:   0.229     R-free:   0.267
Authors: T.Jin,J.Jiang,T.Xiao
Key ref: C.M.Sirois et al. (2013). RAGE is a nucleic acid receptor that promotes inflammatory responses to DNA. J Exp Med, 210, 2447-2463. PubMed id: 24081950 DOI: 10.1084/jem.20120201
Date:
19-Jan-14     Release date:   30-Apr-14    
Supersedes: 3s59
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q15109  (RAGE_HUMAN) -  Advanced glycosylation end product-specific receptor from Homo sapiens
Seq:
Struc:
404 a.a.
211 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

DNA/RNA chains
  C-C-A-T-G-A-C-T-G-T-A-G-G-A-A-A-C-T-C-T-A-G-A 23 bases
  C-T-C-T-A-G-A-G-T-T-T-C-C-T-A-C-A-G-T-C-A-T-G 23 bases

 

 
DOI no: 10.1084/jem.20120201 J Exp Med 210:2447-2463 (2013)
PubMed id: 24081950  
 
 
RAGE is a nucleic acid receptor that promotes inflammatory responses to DNA.
C.M.Sirois, T.Jin, A.L.Miller, D.Bertheloot, H.Nakamura, G.L.Horvath, A.Mian, J.Jiang, J.Schrum, L.Bossaller, K.Pelka, N.Garbi, Y.Brewah, J.Tian, C.Chang, P.S.Chowdhury, G.P.Sims, R.Kolbeck, A.J.Coyle, A.A.Humbles, T.S.Xiao, E.Latz.
 
  ABSTRACT  
 
Recognition of DNA and RNA molecules derived from pathogens or self-antigen is one way the mammalian immune system senses infection and tissue damage. Activation of immune signaling receptors by nucleic acids is controlled by limiting the access of DNA and RNA to intracellular receptors, but the mechanisms by which endosome-resident receptors encounter nucleic acids from the extracellular space are largely undefined. In this study, we show that the receptor for advanced glycation end-products (RAGE) promoted DNA uptake into endosomes and lowered the immune recognition threshold for the activation of Toll-like receptor 9, the principal DNA-recognizing transmembrane signaling receptor. Structural analysis of RAGE-DNA complexes indicated that DNA interacted with dimers of the outermost RAGE extracellular domains, and could induce formation of higher-order receptor complexes. Furthermore, mice deficient in RAGE were unable to mount a typical inflammatory response to DNA in the lung, indicating that RAGE is important for the detection of nucleic acids in vivo.
 

 

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