1jpy
Crystal structure of IL-17F
|
OverviewOverview
The proinflammatory cytokine interleukin 17 (IL-17) is the founding member, of a family of secreted proteins that elicit potent cellular responses. We, report a novel human IL-17 homolog, IL-17F, and show that it is expressed, by activated T cells, can stimulate production of other cytokines such as, IL-6, IL-8 and granulocyte colony-stimulating factor, and can regulate, cartilage matrix turnover. Unexpectedly, the crystal structure of IL-17F, reveals that IL-17 family members adopt a monomer fold typical of cystine, knot growth factors, despite lacking the disulfide responsible for, defining the canonical "knot" structure. IL-17F dimerizes in a parallel, manner like neurotrophins, and features an unusually large cavity on its, surface. Remarkably, this cavity is located in precisely the same position, where nerve growth factor binds its high affinity receptor, TrkA, suggesting further parallels between IL-17s and neurotrophins with respect, to receptor recognition.
About this StructureAbout this Structure
1JPY is a Single protein structure of sequence from Homo sapiens with NDG, NAG and SO4 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding., Hymowitz SG, Filvaroff EH, Yin JP, Lee J, Cai L, Risser P, Maruoka M, Mao W, Foster J, Kelley RF, Pan G, Gurney AL, de Vos AM, Starovasnik MA, EMBO J. 2001 Oct 1;20(19):5332-41. PMID:11574464
Page seeded by OCA on Mon Nov 12 17:43:26 2007