Ontology highlight
ABSTRACT:
SUBMITTER: Finzel BC
PROVIDER: S-EPMC2143846 | biostudies-other | 1998 Oct
REPOSITORIES: biostudies-other
Finzel B C BC Baldwin E T ET Bryant G L GL Hess G F GF Wilks J W JW Trepod C M CM Mott J E JE Marshall V P VP Petzold G L GL Poorman R A RA O'Sullivan T J TJ Schostarez H J HJ Mitchell M A MA
Protein science : a publication of the Protein Society 19981001 10
The binding of two 5-substituted-1,3,4-thiadiazole-2-thione inhibitors to the matrix metalloproteinase stromelysin (MMP-3) have been characterized by protein crystallography. Both inhibitors coordinate to the catalytic zinc cation via an exocyclic sulfur and lay in an unusual position across the unprimed (P1-P3) side of the proteinase active site. Nitrogen atoms in the thiadiazole moiety make specific hydrogen bond interactions with enzyme structural elements that are conserved across all enzyme ...[more]