spacer
spacer

PDBsum entry 4f5e

Go to PDB code: 
protein ligands links
Immune system PDB id
4f5e
Jmol
Contents
Protein chain
186 a.a.
Ligands
EPE
Waters ×31
PDB id:
4f5e
Name: Immune system
Title: Crystal structure of eris/sting
Structure: Transmembrane protein 173. Chain: a. Fragment: unp residues 141-379. Synonym: endoplasmic reticulum interferon stimulator, eris, of irf3 activation, hmita, stimulator of interferon genes p hsting. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: tmem173, eris, mita, sting. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.60Å     R-factor:   0.216     R-free:   0.255
Authors: Y.H.Huang,X.Y.Liu,X.D.Su
Key ref: Y.H.Huang et al. (2012). The structural basis for the sensing and binding of cyclic di-GMP by STING. Nat Struct Mol Biol, 19, 728-730. PubMed id: 22728659
Date:
13-May-12     Release date:   27-Jun-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q86WV6  (TM173_HUMAN) -  Stimulator of interferon genes protein
Seq:
Struc:
379 a.a.
186 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     positive regulation of type I interferon production   2 terms 

 

 
Nat Struct Mol Biol 19:728-730 (2012)
PubMed id: 22728659  
 
 
The structural basis for the sensing and binding of cyclic di-GMP by STING.
Y.H.Huang, X.Y.Liu, X.X.Du, Z.F.Jiang, X.D.Su.
 
  ABSTRACT  
 
STING (stimulator of interferon genes) is an essential signaling adaptor that mediates cytokine production in response to microbial invasion by directly sensing bacterial secondary messengers such as the cyclic dinucleotide bis-(3'-5')-cyclic dimeric GMP (c-di-GMP). STING's structure and its binding mechanism to cyclic dinucleotides were unknown. We report here the crystal structures of the STING cytoplasmic domain and its complex with c-di-GMP, thus providing the structural basis for understanding STING function.