Article
Dynamics of Aromatic Side Chains in the Active Site of FKBP12.
Biochemistry - 10 Jan 2017
Weininger Ulrich, Modig Kristofer, Geitner Anne-Juliane, Schmidpeter Philipp A M, Koch Johanna R, Akke Mikael
Abstract excerpt
FKBP12, a small human enzyme, aids protein folding by catalyzing cis-trans isomerization of peptidyl-prolyl bonds, and is involved in cell signaling pathways, calcium regulation, and the immune response. The underlying molecular mechanisms are not fully understood, but it is well-known that aromatic residues in the active site and neighboring loops are important for substrate binding and catalysis. Here we report...
Topics
- Amino Acids, Aromatic
- Binding Sites
- Catalytic Domain
- Histidine
- Humans
- Hydrogen Bonding
- Isomerism
- Kinetics
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Mutation