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...

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Veröffentlicht in:	Biomolecular NMR assignments 2008-06, Vol.2 (1), p.33-36
Hauptverfasser:	Sauvé, Simon, Gingras, Geneviève, Aubin, Rémy A., Hodgson, Derek J., Aubin, Yves
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Apoptosis Biochemistry Biological and Medical Physics Biophysics Cancer Carbon Isotopes - chemistry Cellular biology Genetics Humans Intracellular Signaling Peptides and Proteins - chemistry Magnetic Resonance Spectroscopy - methods Molecular Sequence Data Molecular Weight Nitrogen Isotopes - chemistry NMR Nuclear magnetic resonance Physics Physics and Astronomy Polymer Sciences Protein Structure, Tertiary Proteins Protons RING Finger Domains Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - chemistry
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Zusammenfassung:	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.
ISSN:	1874-2718 1874-270X
DOI:	10.1007/s12104-007-9077-1