Dimerization of the human cytomegalovirus protease: kinetic and biochemical characterization of the catalytic homodimer.

@article{Margosiak1996DimerizationOT,
  title={Dimerization of the human cytomegalovirus protease: kinetic and biochemical characterization of the catalytic homodimer.},
  author={Stephen A. Margosiak and Darin L. Vanderpool and Wes Sisson and Christopher Pinko and Cornelius C Kan},
  journal={Biochemistry},
  year={1996},
  volume={35 16},
  pages={5300-7}
}
The single-chain 28 kDa human cytomegalovirus (HCMV) protease catalytic domain containing the A143Q mutation has been kinetically and conformationally characterized. The specific activity of the HCMV A143Q protease (HCMVp) increases as the protease concentration increases, suggesting that this protease oligomerizes at high protein concentration to form a more active species. Both cross-linking and light-scattering studies of HCMVp show the existence of a homodimer with an apparent molecular… CONTINUE READING

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