Ontology highlight
ABSTRACT:
SUBMITTER: Lee GM
PROVIDER: S-EPMC3157250 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
Lee Gregory M GM Shahian Tina T Baharuddin Aida A Gable Jonathan E JE Craik Charles S CS
Journal of molecular biology 20110622 5
All members of the human herpesvirus protease (HHV Pr) family are active as weakly associating dimers but inactive as monomers. A small-molecule allosteric inhibitor of Kaposi's sarcoma-associated herpesvirus protease (KSHV Pr) traps the enzyme in an inactive monomeric state where the C-terminal helices are unfolded and the hydrophobic dimer interface is exposed. NMR titration studies demonstrate that the inhibitor binds to KSHV Pr monomers with low micromolar affinity. A 2.0-Å-resolution X-ray ...[more]