NMR assignment of the N-terminal TRAF-like RING zinc finger domain of human FLN29.
Resistance of cancer cells to oncotherapeutics designed to trigger programmed cell death (a.k.a. apoptosis) greatly limits clinical efficacy. The human FLN29 protein may play a role in this process via protein-protein interactions. Here we report the NMR spectral assignment of the N-terminal TRAF2/6-RING-zinc finger-like domain of this protein.
Sauvé
Simon
S
Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, A/L 2201E, Tunney's Pasture, Ottawa, ON, Canada.
Gingras
Geneviève
G
Aubin
Rémy A
RA
Hodgson
Derek J
DJ
Aubin
Yves
Y
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons; D054829:RING Finger Domains; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / Q000737:chemistry*
D002247:Carbon Isotopes; D047908:Intracellular Signaling Peptides and Proteins; D009587:Nitrogen Isotopes; D011522:Protons; C507622:TRAFD1 protein, human; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins