Article
Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.
The EMBO journal - 15 Oct 1997
McCoy M, Stavridi E S, Waterman J L, Wieczorek A M, Opella S J, Halazonetis T D
Abstract excerpt
The p53 tumor suppressor oligomerization domain, a dimer of two primary dimers, is an independently folding domain whose subunits consist of a beta-strand, a tight turn and an alpha-helix. To evaluate the effect of hydrophobic side-chains on three-dimensional structure, we substituted residues Ph...
Topics
- Amino Acid Sequence
- Dimerization
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Protein Binding
- Protein Structure, Secondary
- Tumor Suppressor Protein p53