The NMR structure of the inhibited catalytic domain of human stromelysin-1.
Gooley PR,
O'Connell JF,
Marcy AI,
Cuca GC,
Salowe SP,
Bush BL,
Hermes JD,
Esser CK,
Hagmann WK,
Springer JP, et al.
Department of Biophysical Chemistry, Merck Research Laboratories, Rahway, New Jersey 07065-0900, USA.
The three-dimensional structure of the catalytic domain of stromelysin-1 complexed with an N-carboxyl alkyl inhibitor has been determined by NMR methods. The global fold consists of three helices, a five stranded beta-sheet and a methionine located in a turn near the catalytic histidines, classifying stromelysin-1 as a metzincin. Stromelysin-1 is unique in having two independent zinc binding sites: a catalytic site and a structural site. The inhibitor binds in an extended conformation. The S1' subsite is a deep hydrophobic pocket, whereas S2' appears shallow and S3' open.
PMID: 7656014 [PubMed - indexed for MEDLINE]