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National Academy of Sciences, Proceedings of the National Academy of Sciences, 7(93), p. 2749-2754, 1996

DOI: 10.1073/pnas.93.7.2749

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Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.

Journal article published in 1996 by I. Botos ORCID, L. Scapozza ORCID, D. Zhang, L. A. Liotta, E. F. Meyer
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Matrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metalloproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-angstroms resolution (R = 16.8%). The title structure exhibits an unexpected binding geometry, with the thiophene ring deeply inserted into the primary specificity site. This unprecedented binding geometry dramatizes the significance of the cavernous primary specificity site, pointing the way for the design of a new generation of potential antitumor drugs.