1n1f
From Proteopedia
Crystal Structure of Human Interleukin-19
Structural highlights
FunctionIL19_HUMAN May play some important roles in inflammatory responses. Up-regulates IL-6 and TNF-alpha and induces apoptosis (By similarity). 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 PubMedInterleukin-19 (IL-19) is a novel cytokine that was initially identified during a sequence data base search aimed at finding potential IL-10 homologs. IL-19 shares a receptor complex with IL-20, indicating that the biological activities of these two cytokines overlap and that both may play an important role in regulating development and proper functioning of the skin. We determined the crystal structure of human recombinant IL-19 and refined it at 1.95-A resolution to an R-factor of 0.157. Unlike IL-10, which forms an intercalated dimer, the molecule of IL-19 is a monomer made of seven amphipathic helices, A-G, creating a unique helical bundle. On the basis of the observed structure, we propose that IL-19, IL-20, and other putative members of the proposed IL-10 family together form a distinct subfamily of helical cytokines. Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.,Chang C, Magracheva E, Kozlov S, Fong S, Tobin G, Kotenko S, Wlodawer A, Zdanov A J Biol Chem. 2003 Jan 31;278(5):3308-13. Epub 2002 Oct 25. PMID:12403790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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Categories: Homo sapiens | Large Structures | Chang C | Fong S | Kotenko S | Kozlov S | Magracheva E | Tobin G | Wlodawer A | Zdanov A
