Ontology highlight
ABSTRACT:
SUBMITTER: Huang W
PROVIDER: S-EPMC3623276 | biostudies-literature | 2008 Apr
REPOSITORIES: biostudies-literature
Huang Weijun W Yamamoto Yasufumi Y Li Yi Y Dou Dengfeng D Alliston Kevin R KR Hanzlik Robert P RP Williams Todd D TD Groutas William C WC
Journal of medicinal chemistry 20080305 7
The mechanism of action of a general class of mechanism-based inhibitors of serine proteases, including human neutrophil elastase (HNE), has been elucidated by determining the X-ray crystal structure of an enzyme-inhibitor complex. The captured intermediate indicates that processing of inhibitor by the enzyme generates an N-sulfonyl imine functionality that is tethered to Ser195, in accordance with the postulated mechanism of action of this class of inhibitors. The identity of the HNE-N-sulfonyl ...[more]