Abstract
Cellular FLICE-inhibitory protein (c-FLIP), which is involved in regulating the apoptosis of the extrinsic cell death pathway contains two death effector domains (DED). There are several splicing variants including short-form (c-FLIPS) and long-form (c-FLIPL). The death-inducing signaling complex (DISC) initiates apoptosis and programmed necrosis, DISC assembly and activation are regulated by c-FLIP. Here we report the NMR chemical shift assignments of c-FLIPs, which pave the way for investigating the molecular basis of the anti-apoptotic function of c-FLIPS.
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Acknowledegements
This work was supported by the National Key Research and Development Program of China (No. 2017YFC0906900, 2017YFC1700900), the National Natural Science Foundation of China (No. 21573258) and Shanghai E-Research Institute of Bioactive Constituent in TCM Plan.
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Bai, ZQ., Liu, B., Ma, X. et al. Backbone and side-chain chemical shift assignments of a cellular FLICE-inhibitory protein (c-FLIPS). Biomol NMR Assign 14, 239–243 (2020). https://doi.org/10.1007/s12104-020-09953-8
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DOI: https://doi.org/10.1007/s12104-020-09953-8