Article
Rational design of hirulog-type inhibitors of thrombin.
Journal of computer-aided molecular design - 1 Oct 1994
Egner U, Hoyer G A, Schleuning W D
Abstract excerpt
The two crystal structures of thrombin complexed with its most potent natural inhibitor hirudin and with the active-site inhibitor D-Phe-Pro-Arg-CH2Cl [Rydel, T.J. et al., J. Mol. Biol., 221 (1991) 583; Bode, W. et al., EMBO J., 8 (1989) 3467] were used as a basis to design a new inhibitor, combining the high specificity of the polypeptide hirudin with the simpler chemistry of an organic compound. In the new...
Topics
- Amino Acid Sequence
- Binding Sites
- Computer-Aided Design
- Dipeptides
- Drug Design
- Hirudins
- Humans
- Hydrogen Bonding
- In Vitro Techniques
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure