Mutational analysis and NMR studies of the death domain of the tumor necrosis factor receptor-1

Tumor necrosis factor receptor-1 (TNFR-1) death domain (DD) is the intracellular functional domain responsible for the receptor signaling activities. To understand the transduction mechanism of TNFR-1 signaling we performed structural and functional analysis of the TNFR-DD. The secondary structure o...

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Veröffentlicht in:	Journal of molecular biology 2000-07, Vol.300 (5), p.1323-1333
Hauptverfasser:	Telliez, Jean-Baptiste, Xu, Guang-Yi, Woronicz, John D, Hsu, Sang, Wu, Jing-Lun, Lin, Laura, Sukits, Steven F, Powers, Robert, Lin, Lih-Ling
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution - genetics Antigens, CD - chemistry Antigens, CD - genetics Antigens, CD - metabolism Binding Sites death domain Dimerization Humans Models, Molecular Molecular Sequence Data mutagenesis Nuclear Magnetic Resonance, Biomolecular Osmolar Concentration Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Point Mutation - genetics Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Proteins - chemistry Proteins - metabolism Receptors, Tumor Necrosis Factor - chemistry Receptors, Tumor Necrosis Factor - genetics Receptors, Tumor Necrosis Factor - metabolism Receptors, Tumor Necrosis Factor, Type I Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism secondary structure Sequence Alignment Signal Transduction Structure-Activity Relationship TNF Receptor-Associated Factor 1 TNFR-1 topology
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