spacer
spacer
Go to PDB code: 
protein ligands links
Cytokine PDB id
2ilk
Jmol
Contents
Protein chain
155 a.a. *
Ligands
SO4 ×3
Waters ×303
* Residue conservation analysis
PDB id:
2ilk
Name: Cytokine
Title: Crystal structure of human interleukin-10 at 1.6 angstroms r
Structure: Interleukin-10. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
1.60Å     R-factor:   0.163    
Authors: A.Zdanov,C.Schalk-Hihi,A.Wlodawer
Key ref:
A.Zdanov et al. (1996). Crystal structure of human interleukin-10 at 1.6 A resolution and a model of a complex with its soluble receptor. Protein Sci, 5, 1955-1962. PubMed id: 8897595 Ref: Full text
Date:
01-Jul-96     Release date:   14-Oct-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P22301  (IL10_HUMAN) -  Interleukin-10
Seq:
Struc: 		178 a.a.
155 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   3 terms 
  Biological process     negative regulation of growth of symbiont in host   51 terms 
  Biochemical function     cytokine activity     3 terms  

 

 
Full text Protein Sci 5:1955-1962 (1996)
PubMed id: 8897595  
 
 
Crystal structure of human interleukin-10 at 1.6 A resolution and a model of a complex with its soluble receptor.
A.Zdanov, C.Schalk-Hihi, A.Wlodawer.
 
  ABSTRACT  
 
The crystal structure of human interleukin-10 (IL-10) was refined at 1.6 A resolution against X-ray diffraction data collected at 100 K with the use of synchrotron radiation. Although similar to the IL-10 structure determined previously at room temperature, this low-temperature IL-10 structure contains, in addition, four N-terminal residues, three sulfate anions, and 175 extra water molecules. Whereas the main-chain conformation is preserved, about 30% of the side chains, most of them on the protein surface, assume different conformations. A computer model of a complex of IL-10 with its two soluble receptors was generated based on the topological similarity of IL-10 to interferon-gamma. The contact region between the cytokine and each receptor shows excellent complementarity of polar and hydrophobic interactions, suggesting that the model is generally correct and should be useful in guiding mutagenesis experiments.
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. Distribution of temperature factors (E) inboththe RT an LT (red) structures of E-10. 		Figure 4.
Fig. 4. The 2F0 - F, electrondensitymapscorre- pondingtothedifferentconformations of Leu-13 t RT (bluemap,greencoordinate)andat LT pink map,redcoordinate).
 
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1996, 5, 1955-1962) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21377040 M.Akdis, S.Burgler, R.Crameri, T.Eiwegger, H.Fujita, E.Gomez, S.Klunker, N.Meyer, L.O'Mahony, O.Palomares, C.Rhyner, N.Quaked, A.Schaffartzik, W.Van De Veen, S.Zeller, M.Zimmermann, and C.A.Akdis (2011).
Interleukins, from 1 to 37, and interferon-γ: receptors, functions, and roles in diseases.
  J Allergy Clin Immunol, 127, 701.  
20846897 A.Zdanov (2010).
Structural analysis of cytokines comprising the IL-10 family.
  Cytokine Growth Factor Rev, 21, 325-330.  
20454917 D.B.Trivella, J.R.Ferreira-Júnior, L.Dumoutier, J.C.Renauld, and I.Polikarpov (2010).
Structure and function of interleukin-22 and other members of the interleukin-10 family.
  Cell Mol Life Sci, 67, 2909-2935.  
20712454 H.H.Gad, O.J.Hamming, and R.Hartmann (2010).
The structure of human interferon lambda and what it has taught us.
  J Interferon Cytokine Res, 30, 565-571.  
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.  
18216121 C.Jenkins, W.Garcia, M.J.Godwin, J.V.Spencer, J.L.Stern, A.Abendroth, and B.Slobedman (2008).
Immunomodulatory properties of a viral homolog of human interleukin-10 expressed by human cytomegalovirus during the latent phase of infection.
  J Virol, 82, 3736-3750.  
18024507 M.de Oliveira Neto, J.R.Ferreira, D.Colau, H.Fischer, A.S.Nascimento, A.F.Craievich, L.Dumoutier, J.C.Renauld, and I.Polikarpov (2008).
Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains.
  Biophys J, 94, 1754-1765.  
17238830 J.B.Mumm, S.Ekmekcioglu, N.J.Poindexter, S.Chada, and E.A.Grimm (2006).
Soluble human MDA-7/IL-24: characterization of the molecular form(s) inhibiting tumor growth and stimulating monocytes.
  J Interferon Cytokine Res, 26, 877-886.  
17029234 S.R.McAllister, B.E.Mickus, J.L.Klepeis, and C.A.Floudas (2006).
Novel approach for alpha-helical topology prediction in globular proteins: generation of interhelical restraints.
  Proteins, 65, 930-952.  
15985167 S.Pletnev, E.Magracheva, A.Wlodawer, and A.Zdanov (2005).
A model of the ternary complex of interleukin-10 with its soluble receptors.
  BMC Struct Biol, 5, 10.  
  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.  
  12121653 K.Josephson, B.C.Jones, L.J.Walter, R.DiGiacomo, S.R.Indelicato, and M.R.Walter (2002).
Noncompetitive antibody neutralization of IL-10 revealed by protein engineering and x-ray crystallography.
  Structure, 10, 981-987.
PDB code: 1lk3
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.  
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.  
10494829 J.Grötzinger, T.Kernebeck, K.J.Kallen, and S.Rose-John (1999).
IL-6 type cytokine receptor complexes: hexamer, tetramer or both?
  Biol Chem, 380, 803-813.  
10547147 K.E.Mogensen, M.Lewerenz, J.Reboul, G.Lutfalla, and G.Uzé (1999).
The type I interferon receptor: structure, function, and evolution of a family business.
  J Interferon Cytokine Res, 19, 1069-1098.  
10440995 U.Reineke, J.Schneider-Mergener, R.W.Glaser, R.D.Stigler, M.Seifert, H.D.Volk, and R.Sabat (1999).
Evidence for conformationally different states of interleukin-10: binding of a neutralizing antibody enhances accessibility of a hidden epitope.
  J Mol Recognit, 12, 242-248.  
  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.  
9405662 B.Gesser, H.Leffers, T.Jinquan, C.Vestergaard, N.Kirstein, S.Sindet-Pedersen, S.L.Jensen, K.Thestrup-Pedersen, and C.G.Larsen (1997).
Identification of functional domains on human interleukin 10.
  Proc Natl Acad Sci U S A, 94, 14620-14625.  
  9144766 R.J.Simpson, A.Hammacher, D.K.Smith, J.M.Matthews, and L.D.Ward (1997).
Interleukin-6: structure-function relationships.
  Protein Sci, 6, 929-955.  
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 code is shown on the right.