Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design. [electronic resource]
Producer: 20080108Description: 217-28 p. digitalISSN:- 1089-8638
- Adenosine Triphosphate -- metabolism
- Amino Acid Sequence
- Animals
- Apoenzymes -- chemistry
- Binding Sites
- Catalytic Domain
- Cloning, Molecular
- Crystallography, X-Ray
- Dogs
- Drug Design
- Drug Interactions
- Glutamate-Ammonia Ligase -- chemistry
- Herbicides -- chemical synthesis
- Humans
- Hydrogen Bonding
- Kinetics
- Ligands
- Magnesium -- metabolism
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Pharmaceutical Preparations -- chemical synthesis
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary
- Sequence Homology, Amino Acid
- Substrate Specificity
- Temperature
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
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