Ontology highlight
ABSTRACT:
SUBMITTER: Ung PM
PROVIDER: S-EPMC4136727 | biostudies-literature | 2014 Aug
REPOSITORIES: biostudies-literature
Ung Peter M-U PM Dunbar James B JB Gestwicki Jason E JE Carlson Heather A HA
Journal of medicinal chemistry 20140801 15
NMR and MD simulations have demonstrated that the flaps of HIV-1 protease (HIV-1p) adopt a range of conformations that are coupled with its enzymatic activity. Previously, a model was created for an allosteric site located between the flap and the core of HIV-1p, called the Eye site (Biopolymers 2008, 89, 643-652). Here, results from our first study were combined with a ligand-based, lead-hopping method to identify a novel compound (NIT). NIT inhibits HIV-1p, independent of the presence of an ac ...[more]