Journal article
The NMR structure of the inhibited catalytic domain of human stromelysin-1
PR Gooley, JF O'connell, AI Marcy, GC Cuca, SP Salowe, BL Bush, JD Hermes, CK Esser, WK Hagmann, JP Springer, BA Johnson
Nature Structural Biology | NATURE PUBLISHING CO | Published : 1994
DOI: 10.1038/nsb0294-111
Abstract
The three-dimensional structure of the catalytic domain of stromelysin-1 complexed with an JV-carboxyl alkyl inhibitor has been determined by NMR methods. The global fold consists of three helices, a five stranded β-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 S31 open. © 1994 Nature Publishing Group.