Crystal structure of recombinant human interleukin-22

Autor(es)

Nagem, Ronaldo Alves Pinto ; Colau, Didier ; Dumoutier, Laure ; Renauld, Jean-Christophe ; Ogata, Craig ; Polikarpov, Igor

• Tipo de documento: Artigo Científico
• Fonte: Structure; v. 10, n. 8, p. 1051-1062, Aug. 2002.
• Área do conhecimento: Ciências Biológicas - Bioquímica
• Assunto(s): Peptídeos Interleucinas

Resumo

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)

• Processo FAPESP: 98/06218-6 - Otimização das condições para aquisição de dados de derivados e determinação das fases dos fatores de estrutura de cristais de proteínas através da difração da Luz Síncrotron
• Beneficiário: Ronaldo Alves Pinto Nagem
• Linha de fomento: Bolsas no Brasil - Doutorado
• Processo FAPESP: 99/03387-4 - Estudos estruturais de proteínas usando luz síncrotron
• Beneficiário: Igor Polikarpov
• Linha de fomento: Auxílio à Pesquisa - Temático