Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/57451
Type: Artigo de periódico
Title: Crystal structure of recombinant human interleukin-22
Author: Nagem, RAP
Colau, D
Dumoutier, L
Renauld, JC
Ogata, C
Polikarpov, I
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 I 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 Angstrom 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.
Subject: crystal structure
IL-22
IL-TIF
IL-10
IFN-gamma
interleukin
Country: EUA
Editor: Cell Press
Rights: fechado
Identifier DOI: 10.1016/S0969-2126(02)00797-9
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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