1inr
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Structural highlights
FunctionIL10_HUMAN Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of recombinant human interleukin 10 (rhIL-10) has been determined by X-ray crystallography at 2.0 A resolution. Interleukin 10 is a dimer composed of identical polypeptide chains related by a 2-fold axis. The molecule is predominantly alpha-helical. The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals differences in helix lengths and orientations of the 2-fold related domains. Interleukin 10 and IFN-gamma contain several conserved residues in their internal cores which suggest a possible "fingerprint" for detection of other members of this fold. Crystal structure of interleukin 10 reveals an interferon gamma-like fold.,Walter MR, Nagabhushan TL Biochemistry. 1995 Sep 26;34(38):12118-25. PMID:7547951[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences | ||||||||||||||||||
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