Article
Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain.
The Journal of biological chemistry - 5 Apr 1993
Gaut J R, Hendershot L M
Abstract excerpt
Immunoglobulin-binding protein (BiP), a 70-kDa heat shock protein in the endoplasmic reticulum, binds transiently to nascent proteins, releasing them upon folding and assembly. The in vitro release of bound proteins from BiP requires ATP hydrolysis. Recently, the three-dimensional structure was s...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Animals
- Binding Sites
- Calcium
- Carrier Proteins
- Cell Line
- Consensus Sequence
- Cricetinae
- Endoplasmic Reticulum Chaperone BiP
- Heat-Shock Proteins
- Humans
- Hydrolysis
- Immunoglobulin Heavy Chains
- Mice
- Molecular Chaperones
- Molecular Sequence Data