Ontology highlight
ABSTRACT:
SUBMITTER: Zhou H
PROVIDER: S-EPMC4461556 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
Zhou Hao H Li Shangyang S Badger John J Nalivaika Ellen E Cai Yufeng Y Foulkes-Murzycki Jennifer J Schiffer Celia C Makowski Lee L
Proteins 20150929 11
The flexibility of HIV protease (HIVp) plays a critical role in enabling enzymatic activity and is required for substrate access to the active site. While the importance of flexibility in the flaps that cover the active site is well known, flexibility in other parts of the enzyme is also critical for function. One key region is a loop containing Thr 80, which forms the walls of the active site. Although not situated within the active site, amino acid Thr80 is absolutely conserved. The mutation T ...[more]