NMR resonance assignments of caspase recruitment domain of RIP2 kinase

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• 作者：Zhi Lin
• 关键词：NMR ; Assignment ; CARD ; RIP2
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：10
• 期：2
• 页码：241-244
• 全文大小：640 KB
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X
• 卷排序：10

文摘

Receptor interacting protein-2, RIP2, is a serine/threonine kinase and has sequence homology to RIP. It functions as an adaptor molecule for some members from the tumor necrosis factor receptor family and mediates divergent signaling pathways including NF-κB activation and cell death. RIP2 contains an N-terminal kinases domain and a C-terminal caspase activation and recruitment domain (CARD). The apoptotic activity of RIP2 is restricted to its C-terminal CARD domain while NF-κB activation requires the intact RIP2 for binding. RIP2 CARD involved homotypic or heterotypic interactions with members of the death domains superfamily. Here I report backbone and sidechain 1H, 13C and 15N resonance assignments of soluble RIP2 CARD as a basis for further structural and functional studies.