1m4r | pdb_00001m4r
From Proteopedia
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-22
| ||||||||||||
Structural highlights
Function[IL22_HUMAN] Cytokine that contributes to the inflammatory response in vivo. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInterleukin-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. Crystal structure of recombinant human interleukin-22.,Nagem RA, Colau D, Dumoutier L, Renauld JC, Ogata C, Polikarpov I Structure. 2002 Aug;10(8):1051-62. PMID:12176383[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences | ||||||||||||||||
This page was last modified 08:53, 21 April 2021.