Article
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science (New York, N.Y.) - 15 Jul 1994
Clore G M, Omichinski J G, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn A M
Abstract excerpt
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand...
Topics
- Base Sequence
- Computer Graphics
- DNA
- Genes, p53
- Macromolecular Substances
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Structure, Secondary