Article
A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease.
Proteins - 15 May 2004
Vega Sonia, Kang Lin-Woo, Velazquez-Campoy Adrian, Kiso Yoshiaki, Amzel L Mario, Freire Ernesto
Abstract excerpt
The efficacy of HIV-1 protease inhibition therapies is often compromised by the appearance of mutations in the protease molecule that lower the binding affinity of inhibitors while maintaining viable catalytic activity and substrate affinity. The V82F/I84V double mutation is located within the binding site cavity and affects all protease inhibitors in clinical use. KNI-764, a second-generation inhibitor currently...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.