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Drug Resistance Mutation L76V Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic Contacts

The mature HIV-1 protease (PR) bearing drug-resistance mutation L76V (PR(L76V)) is significantly less stable, with >7-fold higher dimer dissociation constant (K(d)) of 71 ± 24 nM and twice the sensitivity to urea denaturation (UC(50) = 0.85 M) relative to PR. Differential scanning calorimetry sho...

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Détails bibliographiques
Auteurs principaux: Louis, John M., Zhang, Ying, Sayer, Jane M., Wang, Yuan-Fang, Harrison, Robert W., Weber, Irene T.
Format: Artigo
Langue:Inglês
Publié: 2011
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC3101314/
https://ncbi.nlm.nih.gov/pubmed/21446746
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi200033z
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