Article
Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras.
Nature - 12 Dec 1996
Scheffzek K, Lautwein A, Kabsch W, Ahmadian M R, Wittinghofer A
Abstract excerpt
Ras-related GTP-binding proteins function as molecular switches which cycle between GTP-bound 'on'- and GDP-bound 'off'-states. GTP hydrolysis is the common timing mechanism that mediates the return from the 'on' to the 'off'-state. It is usually slow but can be accelerated by orders of magnitude...
Topics
- Amino Acid Sequence
- Catalysis
- Crystallography, X-Ray
- GTP Phosphohydrolases
- GTPase-Activating Proteins
- Guanosine Triphosphate
- Humans
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Protein Conformation
- Protein Folding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Proteins
- Recombinant Proteins
- ras GTPase-Activating Proteins