Backbone and side-chain chemical shift assignments of a cellular FLICE-inhibitory protein (c-FLIPS)

Biomol NMR Assign. 2020 Oct;14(2):239-243. doi: 10.1007/s12104-020-09953-8. Epub 2020 Jun 6.

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.

Keywords: Apoptosis; NMR; c-FLIPS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CASP8 and FADD-Like Apoptosis Regulating Protein / analysis*
  • CASP8 and FADD-Like Apoptosis Regulating Protein / chemistry*
  • Humans
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Proton Magnetic Resonance Spectroscopy

Substances

  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • Nitrogen Isotopes
  • Nitrogen-15