Title : Structural mapping of post-translational modifications in human interleukin-24: role of N-linked glycosylation and disulfide bonds in secretion and activity.

Pub. Date : 2009 Oct 30

PMID : 19734147






3 Functional Relationships(s)
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1 Structural mapping of post-translational modifications in human interleukin-24: role of N-linked glycosylation and disulfide bonds in secretion and activity. Disulfides interleukin 24 Homo sapiens
2 The primary sequence of human IL-24 differs from homologous cytokines, because it possesses three consensus N-linked glycosylation sites and the potential for a single disulfide bond. Disulfides interleukin 24 Homo sapiens
3 These structure-function relationships show that, although IL-24 is a member of the IL-19 subfamily of IL-10-like cytokines by sequence similarity, its surface properties and its distinctive disulfide arrangement make it unique. Disulfides interleukin 24 Homo sapiens