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'''Crystal Structure of Human Interleukin-19''' | '''Crystal Structure of Human Interleukin-19''' | ||
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[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: Zdanov, A.]] | [[Category: Zdanov, A.]] | ||
[[Category: | [[Category: Cytokine]] | ||
[[Category: | [[Category: Four helix bundle]] | ||
[[Category: | [[Category: Interleukin]] | ||
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Revision as of 01:58, 3 May 2008
Crystal Structure of Human Interleukin-19
OverviewOverview
Interleukin-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.
About this StructureAbout this Structure
1N1F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 01:58:13 2008