NMR assignment of the N-terminal TRAF-like RING zinc finger domain of human FLN29

Simon Sauvé; Geneviève Gingras; Rémy A Aubin; Derek J Hodgson; Yves Aubin

doi:10.1007/s12104-007-9077-1

NMR assignment of the N-terminal TRAF-like RING zinc finger domain of human FLN29

Biomol NMR Assign. 2008 Jun;2(1):33-6. doi: 10.1007/s12104-007-9077-1. Epub 2007 Dec 28.

Authors

Simon Sauvé¹, Geneviève Gingras, Rémy A Aubin, Derek J Hodgson, Yves Aubin

Affiliation

¹ 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.

PMID: 19636918
DOI: 10.1007/s12104-007-9077-1

Abstract

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.

MeSH terms

Amino Acid Sequence
Carbon Isotopes / chemistry
Humans
Intracellular Signaling Peptides and Proteins / chemistry*
Magnetic Resonance Spectroscopy / methods*
Molecular Sequence Data
Molecular Weight
Nitrogen Isotopes / chemistry
Protein Structure, Tertiary
Protons
RING Finger Domains*
Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / chemistry*

Substances

Carbon Isotopes
Intracellular Signaling Peptides and Proteins
Nitrogen Isotopes
Protons
TRAFD1 protein, human
Tumor Necrosis Factor Receptor-Associated Peptides and Proteins