Ontology highlight
ABSTRACT:
SUBMITTER: Mittal S
PROVIDER: S-EPMC3391577 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
Mittal Seema S Cai Yufeng Y Nalam Madhavi N L MN Bolon Daniel N A DN Schiffer Celia A CA
Journal of the American Chemical Society 20120228 9
Human immunodeficiency virus Type-1 (HIV-1) protease is crucial for viral maturation and infectivity. Studies of protease dynamics suggest that the rearrangement of the hydrophobic core is essential for enzyme activity. Many mutations in the hydrophobic core are also associated with drug resistance and may modulate the core flexibility. To test the role of flexibility in protease activity, pairs of cysteines were introduced at the interfaces of flexible regions remote from the active site. Disul ...[more]