Ontology highlight
ABSTRACT:
SUBMITTER: Roche J
PROVIDER: S-EPMC4293325 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Chembiochem : a European journal of chemical biology 20141202 2
Flexibility of the glycine-rich flaps is known to be essential for catalytic activity of the HIV-1 protease, but their exact conformations at the different stages of the enzymatic pathway remain subject to much debate. Although hundreds of crystal structures of protease-inhibitor complexes have been solved, only about a dozen inhibitor-free protease structures have been reported. These latter structures reveal a large diversity of flap conformations, ranging from closed to semi-open to wide open ...[more]