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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Crystal structure of recombinant human interleukin-22

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Author(s):
Nagem, Ronaldo Alves Pinto ; Colau, Didier ; Dumoutier, Laure ; Renauld, Jean-Christophe ; Ogata, Craig ; Polikarpov, Igor
Total Authors: 6
Document type: Journal article
Source: Structure; v. 10, n. 8, p. 1051-1062, Aug. 2002.
Field of knowledge: Biological Sciences - Biochemistry
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 Å 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. (AU)

FAPESP's process: 99/03387-4 - Structural studies of the proteins using synchrotron light
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants