Article
The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A.
Structure (London, England : 1993) - 15 Oct 1996
Ryu S E, Choi H J, Kwon K S, Lee K N, Yu M H
Abstract excerpt
BACKGROUND: The protein alpha1-antitrypsin is a prototype member of the serpin (serine protease inhibitor) family and is known to inhibit the activity of neutrophil elastase in the lower respiratory tract. Members of this family undergo a large structural rearrangement upon binding to a target pr...
Topics
- Computer Simulation
- Crystallography, X-Ray
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Serine Proteinase Inhibitors
- alpha 1-Antitrypsin