A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex.

@article{Katoh2003ASN,
  title={A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex.},
  author={Etsuko Katoh and John M. Louis and Toshimasa Yamazaki and Angela M. Gronenborn and Dennis A. Torchia and Rieko Ishima},
  journal={Protein science : a publication of the Protein Society},
  year={2003},
  volume={12 7},
  pages={1376-85}
}
NMR studies of the binding of a substrate to an inactive HIV-1 protease construct, containing an active site mutation PR(D25N), are reported. Substrate titration measurements monitored by HSQC spectra and a (15)N-edited NOESY experiment show that the chromogenic substrate analog of the capsid/p2 cleavage site binds to PR(D25N) with an equilibrium dissociation constant, K(D), of 0.27 +/- 0.05 mM, and upper limits of the association and dissociation rate constants, 2 x 10(4) M(-1)s(-1) and 10 s… CONTINUE READING

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