PDBsum entry: 1m4r

Cytokine

PDB-id

1m4r


	Biological unit* = asymmetric unit, as shown (as deduced by PQS*)

Contents

Description

Header details

Protein chains

Waters ×189

* Residue conservation analysis

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PDB id:

1m4r

Name:

Cytokine

Title:

Crystal structure of recombinant human interleukin-22

Structure:

Interleukin-22. Chain: a, b. Synonym: il-22, il-10-related t-cell-derived inducible factor, il-tif. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biological unit:

Dimer (from PQS)

UniProt:

Chains A, B: Q9GZX6 (IL22_HUMAN)

Seq:

179 a.a.

Struc:

142 a.a.

Key:

Secondary structure

CATH domain

Resolution:

2.00Å

R-factor:

0.188

R-free:

0.220

Authors:

R.A.P.Nagem,D.Colau,L.Dumoutier,J.-C.Renauld,C.Ogata, I.Polikarpov

Key ref:

R.A.Nagem et al. (2002). Crystal structure of recombinant human interleukin-22.. Structure, 10, 1051-1062. [PubMed id: 12176383] [DOI: 10.1016/S0969-2126(02)00797-9]

Date:

03-Jul-02

Release date:

07-Jul-03

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Key reference

DOI no: 10.1016/S0969-2126(02)00797-9 Structure 10:1051-1062 (2002)

PubMed id: 12176383

Crystal structure of recombinant human interleukin-22.

R.A.Nagem, D.Colau, L.Dumoutier, J.C.Renauld, C.Ogata, I.Polikarpov.

ABSTRACT

Interleukin-22 (IL-10-related T cell-derived inducible factor/IL-TIF/IL-22) is a novel cytokine belonging to the IL-10 family. Recombinant human IL-22 (hIL-22) was found to activate the signal transducers and activators of transcription factors 1 and 3 as well as acute phase reactants in several hepatoma cell lines, suggesting its involvement in the inflammatory response. The crystallographic structure of recombinant hIL-22 has been solved at 2.0 A resolution using the SIRAS method. Contrary to IL-10, the hIL-22 dimer does not present an interpenetration of the secondary-structure elements belonging to the two distinct polypeptide chains but results from interface interactions between monomers. Structural differences between these two cytokines, revealed by the crystallographic studies, clearly indicate that, while a homodimer of IL-10 is required for signaling, hIL-22 most probably interacts with its receptor as a monomer.

Selected figure(s)

Figure 3.
Figure 3. The Contact Surface of the hIL-22 DimerThe figure is colored according to residue hydrophobicity (A and B) and electrostatic potential (C and D). Interface views of monomer A (A and C) and monomer B (B and D) are shown. In parts (A) and (B), the darker the yellow, the greater the hydrophobicity. In parts (C) and (D), areas of negative, positive, and neutral electrostatic potential are depicted in red, blue, and white, respectively. The figures were prepared with GRASP [32].

The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 1051-1062) copyright 2002.

Figure was selected by the author.

Literature references that cite this PDB file's key reference

PubMed id Reference

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.

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.

16784489 L.Hummelshoj, L.P.Ryder, and L.K.Poulsen (2006).
The role of the interleukin-10 subfamily members in immunoglobulin production by human B cells.

Scand J Immunol, 64, 40-47.

16982608 S.I.Yoon, N.J.Logsdon, F.Sheikh, R.P.Donnelly, and M.R.Walter (2006).
Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex.

J Biol Chem, 281, 35088-35096.

PDB code: 2h24

15618397 J.Klein, and N.Nikolaidis (2005).
The descent of the antibody-based immune system by gradual evolution.

Proc Natl Acad Sci U S A, 102, 169-174.

15983417 T.Xu, N.J.Logsdon, and M.R.Walter (2005).
Structure of insect-cell-derived IL-22.

Acta Crystallogr D Biol Crystallogr, 61, 942-950.

PDB code: 1ykb

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.

15213397 T.Xu, N.J.Logsdon, and M.R.Walter (2004).
Crystallization and X-ray diffraction analysis of insect-cell-derived IL-22.

Acta Crystallogr D Biol Crystallogr, 60, 1295-1298.

12667095 B.E.Rich (2003).
IL-20: a new target for the treatment of inflammatory skin disease.

Expert Opin Ther Targets, 7, 165-174.

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

12974481 J.C.Renauld (2003).
Class II cytokine receptors and their ligands: key antiviral and inflammatory modulators.

Nat Rev Immunol, 3, 667-676.

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.