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Cytokine PDB id
1ykb
Jmol
Contents
Protein chains
(+ 0 more) 141 a.a. *
Ligands
NAG-FUC-NAG
NAG ×3
NAG-NAG ×4
NAG-NAG-MAN-MAN-
FUC
Waters ×51
* Residue conservation analysis
PDB id:
1ykb
Name: Cytokine
Title: Crystal structure of insect cell expressed il-22
Structure: Protein (interleukin-22). Chain: a, b, c, d, e, f. Synonym: il-22, il-10-related t-cell-derived inducible fact tif, unq3099/pro10096. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: il22, iltif.
Biol. unit: Dimer (from PQS)
Resolution:
2.60Å     R-factor:   0.232     R-free:   0.265
Authors: T.Xu,N.J.Logsdon,M.R.Walter
Key ref:
T.Xu et al. (2005). Structure of insect-cell-derived IL-22. Acta Crystallogr D Biol Crystallogr, 61, 942-950. PubMed id: 15983417 DOI: 10.1107/S0907444905009601
Date:
17-Jan-05     Release date:   12-Jul-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9GZX6  (IL22_HUMAN) -  Interleukin-22
Seq:
Struc: 		179 a.a.
141 a.a.
Key:    PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     cell-cell signaling   3 terms 
  Biochemical function     cytokine activity     2 terms  

 

 
DOI no: 10.1107/S0907444905009601 Acta Crystallogr D Biol Crystallogr 61:942-950 (2005)
PubMed id: 15983417  
 
 
Structure of insect-cell-derived IL-22.
T.Xu, N.J.Logsdon, M.R.Walter.
 
  ABSTRACT  
 
The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm)) has been determined at 2.6 A resolution. IL-22(Dm) crystals contain six molecules in the asymmetric unit. Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine. However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites. The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Schematic model of the IL-22/IL-22R1/IL-10R1 signaling complex. IL-22-mediated assembly of the ternary receptor complex activates both JAK/STAT and MAP kinase signaling pathways (Lejeune et al., 2002[80] [Lejeune, D., Dumoutier, L., Constantinescu, S., Kruijer, W., Schuringa, J. J. & Renauld, J. C. (2002). J. Biol. Chem. 277, 33686-33682.]-[81][bluearr.gif] ). Only the JAK kinases and STAT3 are shown in the figure, although IL-22 also activates STAT1 and STAT5 at reduced levels (Lejeune et al., 2002[82] [Lejeune, D., Dumoutier, L., Constantinescu, S., Kruijer, W., Schuringa, J. J. & Renauld, J. C. (2002). J. Biol. Chem. 277, 33686-33682.]-[83][bluearr.gif] ). Fluorescence resonance energy transfer (FRET) data collected on the IFN- [84][gamma] receptor complex suggests that class-2 cytokines induce signaling by separating the intracellular domains of the receptors (Krause et al., 2002[85] [Krause, C. D., Mei, E., Xie, J., Jia, Y., Bopp, M. A., Hochstrasser, R. M. & Pestka, S. (2002). Mol. Cell Proteomics, 1, 805-815.]-[86][bluearr.gif] ). IL-22 receptor-complex assembly activates the JAK kinases, resulting in phosphorylation of IL-22R1, JAK1, TYK2 and STAT3. Phosphorylated STAT3 dimers translocate to the nucleus where they activate gene transcription, resulting in IL-22 cellular responses. The orientation of Figs. 2[87] [link]-[88][turqarr.gif] (a) and 8[89] [link]-[90][turqarr.gif] are shown on the complex by an arrow. The view in Fig. 7[91] [link]-[92][turqarr.gif] corresponds to the box shown in the figure. The color codes for the receptors and IL-22 are shown in the figure. 		Figure 2.
Figure 2 Structure of IL-22[Dm]. (a) Ribbon diagram of the IL-22[Dm] monomer. Asparagines that are modified by N-linked glycosylation are shown. The boxed region corresponds to the region shown in Fig. 3[152] [link]-[153][turqarr.gif] . (b) Packing in the asymmetric unit of the IL-22[Dm] cell. Ribbon diagram of the six NCS-related IL-22[Dm] monomers labeled by chain identifier (A-F). N-linked glycosylation attached to each monomer is shown in space-filling format and colored the same as the ribbon to which it is attached.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2005, 61, 942-950) copyright 2005.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20445503 A.De Luca, T.Zelante, C.D'Angelo, S.Zagarella, F.Fallarino, A.Spreca, R.G.Iannitti, P.Bonifazi, J.C.Renauld, F.Bistoni, P.Puccetti, and L.Romani (2010).
IL-22 defines a novel immune pathway of antifungal resistance.
  Mucosal Immunol, 3, 361-373.  
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.  
20127093 K.Wolk, E.Witte, K.Witte, K.Warszawska, and R.Sabat (2010).
Biology of interleukin-22.
  Semin Immunopathol, 32, 17-31.  
20947410 R.P.Donnelly, F.Sheikh, H.Dickensheets, R.Savan, H.A.Young, and M.R.Walter (2010).
Interleukin-26: an IL-10-related cytokine produced by Th17 cells.
  Cytokine Growth Factor Rev, 21, 393-401.  
21112807 R.Sabat (2010).
IL-10 family of cytokines.
  Cytokine Growth Factor Rev, 21, 315-324.  
19734147 K.L.Fuson, M.Zheng, M.Craxton, A.Pataer, R.Ramesh, S.Chada, and R.B.Sutton (2009).
Structural mapping of post-translational modifications in human interleukin-24: role of N-linked glycosylation and disulfide bonds in secretion and activity.
  J Biol Chem, 284, 30526-30533.  
  19193995 L.Watanabe, P.R.de Moura, A.S.Nascimento, D.Colau, L.Dumoutier, J.C.Renauld, and I.Polikarpov (2009).
Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to its soluble decoy receptor IL-22BP.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 102-104.  
  18391423 B.C.Jones, N.J.Logsdon, and M.R.Walter (2008).
Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to the extracellular IL-22R1 chain.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 266-269.  
18599299 B.C.Jones, N.J.Logsdon, and M.R.Walter (2008).
Structure of IL-22 bound to its high-affinity IL-22R1 chain.
  Structure, 16, 1333-1344.
PDB code: 3dgc
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.  
17030002 K.Wolk, and R.Sabat (2006).
Interleukin-22: a novel T- and NK-cell derived cytokine that regulates the biology of tissue cells.
  Cytokine Growth Factor Rev, 17, 367-380.  
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.