The NMR structure of the inhibited catalytic domain of human stromelysin–1
- 1 February 1994
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 1 (2), 111-118
- https://doi.org/10.1038/nsb0294-111
Abstract
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.Keywords
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