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Cytokine PDB id
1vlk
Jmol
Contents
Protein chain
142 a.a. *
Waters ×75
* Residue conservation analysis
PDB id:
1vlk
Name: Cytokine
Title: Structure of viral interleukin-10
Structure: Viral interleukin-10. Chain: a. Synonym: bcrf1 protein. Engineered: yes
Source: Human herpesvirus 4. Epstein-barr virus. Organism_taxid: 10376. Strain: gd1. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PDB file)
Resolution:
1.90Å     R-factor:   0.191    
Authors: A.Zdanov,C.Schalk-Hihi,A.Wlodawer
Key ref:
A.Zdanov et al. (1997). Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10. J Mol Biol, 268, 460-467. PubMed id: 9159483 DOI: 10.1006/jmbi.1997.0990
Date:
14-Feb-97     Release date:   01-Apr-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P03180  (IL10H_EBVB9) -  Viral interleukin-10 homolog
Seq:
Struc: 		170 a.a.
142 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     immune response   3 terms 
  Biochemical function     protein binding     2 terms  

 

 
DOI no: 10.1006/jmbi.1997.0990 J Mol Biol 268:460-467 (1997)
PubMed id: 9159483  
 
 
Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10.
A.Zdanov, C.Schalk-Hihi, S.Menon, K.W.Moore, A.Wlodawer.
 
  ABSTRACT  
 
The crystal structure of Epstein-Barr virus protein BCRF1, an analog of cellular interleukin-10 (IL-10), has been determined at the resolution of 1.9 A and refined to an R-factor 0.191. The structure of this cytokine is similar to that of human IL-10 (hIL-10), forming an intercalated dimer of two 17 kDa polypeptides related by a crystallographic 2-fold symmetry axis. BCRF1 exhibits novel conformations of the N-terminal coil and of the loop between helices A and B compared to hIL-10. These regions are likely to be involved in binding of one or more components of the IL-10 receptor system, and thus the structural differences may account for the lower binding affinity and limited spectrum of biological activities of viral IL-10, compared to hIL-10.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. The alignment of amino acid sequences of viral and human IL-10. Identical residues are shown in red, similar residues in blue. 		Figure 4.
Figure 4. A putative receptor binding site in IL-10. Here vIL-10 is shown in blue, hIL-10 in white, the hydrophobic patch residues are in green, and polar residues in orange.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1997, 268, 460-467) copyright 1997.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20714339 A.E.Serrano, E.Menares-Castillo, M.Garrido-Tapia, C.H.Ribeiro, C.J.Hernández, A.Mendoza-Naranjo, M.Gatica-Andrades, R.Valenzuela-Diaz, R.Zúñiga, M.N.López, F.Salazar-Onfray, J.C.Aguillón, and M.C.Molina (2011).
Interleukin 10 decreases MICA expression on melanoma cell surface.
  Immunol Cell Biol, 89, 447-457.  
21328379 Y.Chao, Y.Jing, Y.Jia, Y.Wang, C.Zhao, and B.Luo (2011).
Conservation and mutation of viral interleukin-10 gene in gastric carcinomas and nasopharyngeal carcinomas.
  J Med Virol, 83, 644-650.  
20846897 A.Zdanov (2010).
Structural analysis of cytokines comprising the IL-10 family.
  Cytokine Growth Factor Rev, 21, 325-330.  
21115385 R.Sabat, G.Grütz, K.Warszawska, S.Kirsch, E.Witte, K.Wolk, and J.Geginat (2010).
Biology of interleukin-10.
  Cytokine Growth Factor Rev, 21, 331-344.  
19640997 B.Slobedman, P.A.Barry, J.V.Spencer, S.Avdic, and A.Abendroth (2009).
Virus-encoded homologs of cellular interleukin-10 and their control of host immune function.
  J Virol, 83, 9618-9629.  
19298643 L.Bortesi, M.Rossato, F.Schuster, N.Raven, J.Stadlmann, L.Avesani, A.Falorni, F.Bazzoni, R.Bock, S.Schillberg, and M.Pezzotti (2009).
Viral and murine interleukin-10 are correctly processed and retain their biological activity when produced in tobacco.
  BMC Biotechnol, 9, 22.  
  18296259 A.Pietrzak, A.Zalewska, G.Chodorowska, P.Nockowski, A.Michalak-Stoma, P.Osemlak, and D.Krasowska (2008).
Genes and structure of selected cytokines involved in pathogenesis of psoriasis.
  Folia Histochem Cytobiol, 46, 11-21.  
18652995 P.Van de Perre, M.Segondy, V.Foulongne, A.Ouedraogo, I.Konate, J.M.Huraux, P.Mayaud, and N.Nagot (2008).
Herpes simplex virus and HIV-1: deciphering viral synergy.
  Lancet Infect Dis, 8, 490-497.  
17763933 K.Kanai, Y.Satoh, H.Yamanaka, A.Kawaguchi, K.Horie, K.Sugata, Y.Hoshikawa, T.Sata, and T.Sairenji (2007).
The vIL-10 gene of the Epstein-Barr virus (EBV) is conserved in a stable manner except for a few point mutations in various EBV isolates.
  Virus Genes, 35, 563-569.  
17224278 S.I.Yoon, and M.R.Walter (2007).
Identification and characterization of a +1 frameshift observed during the expression of Epstein-Barr virus IL-10 in Escherichia coli.
  Protein Expr Purif, 53, 132-137.  
15837194 S.I.Yoon, B.C.Jones, N.J.Logsdon, and M.R.Walter (2005).
Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain.
  Structure, 13, 551-564.
PDB codes: 1y6k 1y6m 1y6n
15032600 S.Pestka, C.D.Krause, D.Sarkar, M.R.Walter, Y.Shi, and P.B.Fisher (2004).
Interleukin-10 and related cytokines and receptors.
  Annu Rev Immunol, 22, 929-979.  
12403790 C.Chang, E.Magracheva, S.Kozlov, S.Fong, G.Tobin, S.Kotenko, A.Wlodawer, and A.Zdanov (2003).
Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.
  J Biol Chem, 278, 3308-3313.
PDB code: 1n1f
14622251 R.Savan, D.Igawa, and M.Sakai (2003).
Cloning, characterization and expression analysis of interleukin-10 from the common carp, Cyprinus carpio L.
  Eur J Biochem, 270, 4647-4654.  
12093920 B.C.Jones, N.J.Logsdon, K.Josephson, J.Cook, P.A.Barry, and M.R.Walter (2002).
Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1.
  Proc Natl Acad Sci U S A, 99, 9404-9409.
PDB code: 1lqs
  11929132 H.Fickenscher, S.Hör, H.Küpers, A.Knappe, S.Wittmann, and H.Sticht (2002).
The interleukin-10 family of cytokines.
  Trends Immunol, 23, 89-96.  
11970958 K.Vandenbroeck, I.Alloza, D.Brehmer, A.Billiau, P.Proost, N.McFerran, S.Rüdiger, and B.Walker (2002).
The conserved helix C region in the superfamily of interferon-gamma /interleukin-10-related cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK.
  J Biol Chem, 277, 25668-25676.  
11498300 B.E.Gewurz, R.Gaudet, D.Tortorella, E.W.Wang, and H.L.Ploegh (2001).
Virus subversion of immunity: a structural perspective.
  Curr Opin Immunol, 13, 442-450.  
11244051 K.W.Moore, R.de Waal Malefyt, R.L.Coffman, and A.O'Garra (2001).
Interleukin-10 and the interleukin-10 receptor.
  Annu Rev Immunol, 19, 683-765.  
10729163 A.Knappe, S.Hör, S.Wittmann, and H.Fickenscher (2000).
Induction of a novel cellular homolog of interleukin-10, AK155, by transformation of T lymphocytes with herpesvirus saimiri.
  J Virol, 74, 3881-3887.  
11060663 K.Asadullah, W.D.Döcke, R.V.Sabat, H.D.Volk, and W.Sterry (2000).
The treatment of psoriasis with IL-10: rationale and review of the first clinical trials.
  Expert Opin Investig Drugs, 9, 95.  
10677520 S.V.Kotenko, S.Saccani, L.S.Izotova, O.V.Mirochnitchenko, and S.Pestka (2000).
Human cytomegalovirus harbors its own unique IL-10 homolog (cmvIL-10).
  Proc Natl Acad Sci U S A, 97, 1695-1700.  
10637267 Y.Ding, L.Qin, S.V.Kotenko, S.Pestka, and J.S.Bromberg (2000).
A single amino acid determines the immunostimulatory activity of interleukin 10.
  J Exp Med, 191, 213-224.  
10231374 D.M.Hoover, C.Schalk-Hihi, C.C.Chou, S.Menon, A.Wlodawer, and A.Zdanov (1999).
Purification of receptor complexes of interleukin-10 stoichiometry and the importance of deglycosylation in their crystallization.
  Eur J Biochem, 262, 134-141.  
10399060 F.M.Brodsky (1999).
Stealth, sabotage and exploitation.
  Immunol Rev, 168, 5.  
9535648 H.L.Ploegh (1998).
Viral strategies of immune evasion.
  Science, 280, 248-253.  
9692957 J.M.Matthews, A.Hammacher, G.J.Howlett, and R.J.Simpson (1998).
Physicochemical characterization of an antagonistic human interleukin-6 dimer.
  Biochemistry, 37, 10671-10680.  
  9568901 U.Reineke, R.Sabat, H.D.Volk, and J.Schneider-Mergener (1998).
Mapping of the interleukin-10/interleukin-10 receptor combining site.
  Protein Sci, 7, 951-960.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.