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- W2775690235 abstract "Significance Innate immune signaling has an essential role in inflammation, and dysfunction of signaling components in these pathways contributes to autoimmunity and cancer. Interleukin-1 receptor-associated kinase (IRAK) family members are key mediators of signal transduction by Toll-like receptors and Interleukin-1 receptors in innate immunity and therefore serve as potential therapeutic targets for these diseases. The crystal structure of the IRAK1 kinase domain in complex with a small molecule inhibitor reveals important structural details of the kinase that provide insights into the design of selective IRAK inhibitors. Characterization of IRAK1 heterodimerization with the upstream kinase IRAK4 suggests a mechanism of IRAK1 activation by IRAK4." @default.
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- W2775690235 date "2017-12-05" @default.
- W2775690235 modified "2023-10-05" @default.
- W2775690235 title "Crystal structure of human IRAK1" @default.
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- W2775690235 doi "https://doi.org/10.1073/pnas.1714386114" @default.
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