Background: The protein α1-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 protease, involving cleavage of the reactive-site loop. This loop is then inserted into the main body of the enzyme following the opening of a central β sheet, leading to stabilization of the structure. Random mutageneses of α1-antitrypsin identified various mutations that stabilize the native structure and retard the insertion of the reactive-site loop. Structural studies of these mutations may reveal the mechanism of the conformational change. Results: ...
Metastability of the native form of proteins has been recognized as a mechanism of biological regula...
The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state,...
The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state,...
Background: The protein α1-antitrypsin is a prototype member of the serpin (serine protease inhibito...
AbstractBackground The protein α1-antitrypsin is a prototype member of the serpin (serine protease i...
AbstractBackground The protein α1-antitrypsin is a prototype member of the serpin (serine protease i...
Serine protease inhibitors (serpins) are metastable in their native state. This strain, which is rel...
Serine protease inhibitors (serpins) are metastable in their native state. This strain, which is rel...
The metastability of inhibitory serpins (serine proteinase inhibitors) is thought to play a key role...
The metastability of inhibitory serpins (serine proteinase inhibitors) is thought to play a key role...
The metastability of inhibitory serpins (serine proteinase inhibitors) is thought to play a key role...
α(1)-Antitrypsin, the archetypal member of the serpin superfamily, is a metastable protein prone to ...
The conformational plasticity of serpins underlies both their activities as protease inhibitors and ...
Metastability of the native form of proteins has been recognized as a mechanism of biological regula...
Metastability of the native form of proteins has been recognized as a mechanism of biological regula...
Metastability of the native form of proteins has been recognized as a mechanism of biological regula...
The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state,...
The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state,...
Background: The protein α1-antitrypsin is a prototype member of the serpin (serine protease inhibito...
AbstractBackground The protein α1-antitrypsin is a prototype member of the serpin (serine protease i...
AbstractBackground The protein α1-antitrypsin is a prototype member of the serpin (serine protease i...
Serine protease inhibitors (serpins) are metastable in their native state. This strain, which is rel...
Serine protease inhibitors (serpins) are metastable in their native state. This strain, which is rel...
The metastability of inhibitory serpins (serine proteinase inhibitors) is thought to play a key role...
The metastability of inhibitory serpins (serine proteinase inhibitors) is thought to play a key role...
The metastability of inhibitory serpins (serine proteinase inhibitors) is thought to play a key role...
α(1)-Antitrypsin, the archetypal member of the serpin superfamily, is a metastable protein prone to ...
The conformational plasticity of serpins underlies both their activities as protease inhibitors and ...
Metastability of the native form of proteins has been recognized as a mechanism of biological regula...
Metastability of the native form of proteins has been recognized as a mechanism of biological regula...
Metastability of the native form of proteins has been recognized as a mechanism of biological regula...
The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state,...
The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state,...