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Comparative Study
. 1994 Feb;1(2):111-8.
doi: 10.1038/nsb0294-111.

The NMR structure of the inhibited catalytic domain of human stromelysin-1

P R Gooley  1 , J F O'Connell, A I Marcy, G C Cuca, S P Salowe, B L Bush, J D Hermes, C K Esser, W K Hagmann, J P Springer, et al.
Affiliations
Comparative Study

The NMR structure of the inhibited catalytic domain of human stromelysin-1

P R Gooley et al. Nat Struct Biol. 1994 Feb.

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.

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