Solution structure of the tetrameric minimum transforming domain of p53

We report the solution structure of the minimum transforming domain (residues 303–366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of important functions associated with p53 activity including transformation, oligomerization, nuclear localizat...

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Veröffentlicht in:	Nature Structural Biology 1994-12, Vol.1 (12), p.877-890
Hauptverfasser:	Lee, Weontae, Harvey, Timothy S, Yin, Ya, Yau, Patrick, Litchfield, David, Arrowsmith, Cheryl H
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences DNA - chemistry DNA - metabolism Humans Life Sciences Magnetic Resonance Spectroscopy Membrane Biology Models, Molecular Molecular Sequence Data Molecular Structure Nucleic Acid Conformation Phosphorylation Protein Binding Protein Conformation Protein Structure Protein Structure, Secondary Solutions Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism
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