Probing the role of two hydrophobic active site residues in the human dihydrofolate reductase by site-directed mutagenesis.

@article{Schweitzer1989ProbingTR,
  title={Probing the role of two hydrophobic active site residues in the human dihydrofolate reductase by site-directed mutagenesis.},
  author={B. Schweitzer and S. Srimatkandada and H. Gritsman and R. Sheridan and R. Venkataraghavan and J. Bertino},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 34},
  pages={
          20786-95
        }
}
In the x-ray structure of the human dihydrofolate reductase, phenylalanine 31 and phenylalanine 34 have been shown to be involved in hydrophobic interactions with bound substrates and inhibitors. Using oligonucleotide-directed mutagenesis and a bacterial expression system producing the wild-type and mutant human dihydrofolate reductases at levels of 10% of the bacterial protein, we have constructed, expressed, and purified a serine 31 (S31) mutant and a serine 34 (S34) mutant. Fluorescence… Expand
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