1DTH

METALLOPROTEASE

Summary for 1DTH

• Entry DOI: 10.2210/pdb1dth/pdb
• Descriptor: ATROLYSIN C, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, metalloprotease, zinc, venom
• Biological source: Crotalus atrox (western diamondback rattlesnake)
• Cellular location: Secreted: P15167
• Total number of polymer chains: 2
• Total formula weight: 47717.02

Authors

Botos, I.,Scapozza, L.,Zhang, D.,Liotta, L.A.,Meyer, E.F. (deposition date: 1996-02-12, release date: 1997-02-12, Last modification date: 2024-10-30)

Primary citation

Botos, I.,Scapozza, L.,Zhang, D.,Liotta, L.A.,Meyer, E.F.
Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Proc.Natl.Acad.Sci.USA, 93:2749-2754, 1996

PubMed 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.

PubMed: 8610113
DOI: 10.1073/pnas.93.7.2749

Experimental method

X-RAY DIFFRACTION (2 Å)