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PDBsum entry 4xfs

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protein ligands Protein-protein interface(s) links
Cytokine PDB id
4xfs

 

 

 

 

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Contents
Protein chains
156 a.a.
Ligands
DMS ×5
GOL ×2
Waters ×103
PDB id:
4xfs
Name: Cytokine
Title: Structure of il-18 ser mutant i
Structure: Interleukin-18. Chain: a, b. Synonym: il-18,iboctadekin,interferon gamma-inducing factor,ifn- gamma-inducing factor,interleukin-1 gamma,il-1 gamma. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: il18, igif, il1f4. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.91Å     R-factor:   0.181     R-free:   0.229
Authors: B.E.Krumm,X.Meng,Y.Xiang,J.Deng
Key ref: B.Krumm et al. (2015). Crystallization of interleukin-18 for structure-based inhibitor design. Acta Crystallogr F Struct Biol Commun, 71, 710-717. PubMed id: 26057800 DOI: 10.1107/S2053230X15006871
Date:
29-Dec-14     Release date:   10-Jun-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q14116  (IL18_HUMAN) -  Interleukin-18 from Homo sapiens
Seq:
Struc:
193 a.a.
156 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 

 
DOI no: 10.1107/S2053230X15006871 Acta Crystallogr F Struct Biol Commun 71:710-717 (2015)
PubMed id: 26057800  
 
 
Crystallization of interleukin-18 for structure-based inhibitor design.
B.Krumm, X.Meng, Y.Xiang, J.Deng.
 
  ABSTRACT  
 
Interleukin-18 (IL-18) is a pleiotropic pro-inflammatory cytokine belonging to the IL-1 superfamily. IL-18 plays an important role in host innate and acquired immune defense, with its activity being modulated in vivo by its naturally occurring antagonist IL-18 binding protein (IL-18BP). Recent crystal structures of human IL-18 (hIL-18) in complex with its antagonist or cognate receptor(s) have revealed a conserved binding interface on hIL-18 representing a promising drug target. An important step in this process is obtaining crystals of apo hIL-18 or hIL-18 in complex with small-molecule inhibitors, preferably under low ionic strength conditions. In this study, surface-entropy reduction (SER) and rational protein design were employed to facilitate the crystallization of hIL-18. The results provide an excellent platform for structure-based drug design.
 

 

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