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

Nature Structural Biology volume 1, pages 111–118 (1994)Cite this article

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 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 S3′ open.

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Authors and Affiliations

  1. Department of Biophysical Chemistry, Merck Research Laboratories, P.O. Box 2000, Rahway, New Jersey, 07065-0900

    Paul R. Gooley, John F. O'Connell, Alice I. Marcy, Gregory C. Cuca, Scott P. Salowe, Bruce L. Bush, Jeffrey D. Hermes, James P. Springer & Bruce A. Johnson

  2. Medicinal Chemical Research, Merck Research Laboratories, P.O. Box 2000, Rahway, New Jersey, 07065-0900

    Craig K. Esser & William K. Hagmann

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Gooley, P., O'Connell, J., Marcy, A. et al. The NMR structure of the inhibited catalytic domain of human stromelysin–1. Nat Struct Mol Biol 1, 111–118 (1994). https://doi.org/10.1038/nsb0294-111

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