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Cytokine PDB id
1icw
Jmol
Contents
Protein chains
69 a.a. *
Waters ×52
* Residue conservation analysis
PDB id:
1icw
Name: Cytokine
Title: Interleukin-8, mutant with glu 38 replaced by cys and cys 50 replaced by ala
Structure: Interleukin-8. Chain: a, b. Synonym: il-8. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.01Å     R-factor:   0.194     R-free:   0.266
Authors: C.Eigenbrot,H.B.Lowman,L.Chee,D.R.Artis
Key ref: C.Eigenbrot et al. (1997). Structural change and receptor binding in a chemokine mutant with a rearranged disulfide: X-ray structure of E38C/C50AIL-8 at 2 A resolution. Proteins, 27, 556-566. PubMed id: 9141135 DOI: 10.1002/(SICI)1097-0134(199704)27:4<556::AID-PROT8>3.3.CO;2-S
Date:
18-Sep-96     Release date:   12-Mar-97    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P10145  (IL8_HUMAN) -  Interleukin-8
Seq:
Struc: 		99 a.a.
69 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!
  Cellular component     extracellular region   3 terms 
  Biological process     intracellular signal transduction   21 terms 
  Biochemical function     protein binding     4 terms  

 

 
DOI no: 10.1002/(SICI)1097-0134(199704)27:4<556::AID-PROT8>3.3.CO;2-S Proteins 27:556-566 (1997)
PubMed id: 9141135  
 
 
Structural change and receptor binding in a chemokine mutant with a rearranged disulfide: X-ray structure of E38C/C50AIL-8 at 2 A resolution.
C.Eigenbrot, H.B.Lowman, L.Chee, D.R.Artis.
 
  ABSTRACT  
 
The characteristic CXC chemokine disulfide core of interleukin-8 (IL-8) has been rearranged in a variant replacing the 9-50 disulfide with a 9-38 disulfide. The new variant has been characterized by its binding affinity to IL-8 receptors A and B and the erythrocyte receptor DARC. This variant binds the three receptors with affinities between 500- and 2,500-fold lower than wild-type IL-8. Binding affinity results are also reported for the variant with alanine substituted for both cysteines 9 and 50. The Glu38-->Cys/Cys50-->Ala IL-8 crystallizes in space group P2(1)2(1)2(1) with cell parameters a = 46.4, b = 49.2, and c = 69.5 A, and has been refined to an R-value of 19.4% for data from 10 to 2 A resolution. Analysis of the structure confirms the new disulfide arrangement and suggests that changes at Ile10 may be the principal cause of the lowered affinities.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
11807180 E.J.Fernandez, and E.Lolis (2002).
Structure, function, and inhibition of chemokines.
  Annu Rev Pharmacol Toxicol, 42, 469-499.  
  11152129 Buyong, J.Xiong, J.Lubkowski, and R.Nussinov (2000).
Homology modeling and molecular dynamics simulations of lymphotactin.
  Protein Sci, 9, 2192-2199.  
10707023 N.Gerber, H.Lowman, D.R.Artis, and C.Eigenbrot (2000).
Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution.
  Proteins, 38, 361-367.
PDB code: 1qe6
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