Article
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
The EMBO journal - 1 Sept 1994
Fogh R H, Ottleben G, Rüterjans H, Schnarr M, Boelens R, Kaptein R
Abstract excerpt
The structure of the 84 residue DNA binding domain of the Escherichia coli LexA repressor has been determined from NMR data using distance geometry and restrained molecular dynamics. The assignment of the 1H NMR spectrum of the molecule, derived from 2- and 3-D homonuclear experiments, is also re...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Binding Sites
- Computer Simulation
- DNA
- Escherichia coli
- Helix-Loop-Helix Motifs
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Protein Conformation
- Repressor Proteins
- Sequence Homology, Amino Acid
- Serine Endopeptidases
- Solutions