1ATL

Structural interaction of natural and synthetic inhibitors with the VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)

Summary for 1ATL

• Entry DOI: 10.2210/pdb1atl/pdb
• Descriptor: Snake venom metalloproteinase atrolysin-D, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: metalloendopeptidase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Crotalus atrox (Western diamondback rattlesnake)
• Total number of polymer chains: 2
• Total formula weight: 47184.38

Authors

Zhang, D.,Botos, I.,Gomis-Rueth, F.-X.,Doll, R.,Blood, C.,Njoroge, F.G.,Fox, J.W.,Bode, W.,Meyer, E.F. (deposition date: 1995-05-26, release date: 1995-10-15, Last modification date: 2024-10-23)

Primary citation

Zhang, D.,Botos, I.,Gomis-Ruth, F.X.,Doll, R.,Blood, C.,Njoroge, F.G.,Fox, J.W.,Bode, W.,Meyer, E.F.
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Proc.Natl.Acad.Sci.USA, 91:8447-8451, 1994

PubMed Abstract: The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC 3.4.24.42), from the venom of the western diamondback rattlesnake Crotalus atrox, has been determined to atomic resolution by x-ray crystallographic methods. This study illuminates the nature of inhibitor binding with natural (< Glu-Asn-Trp, where < Glu is pyroglutamic acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is exceptionally deep; the nature of inhibitor and productive substrate binding is discussed. Insights gained from the study of these complexes facilitate the design of potential drugs to treat diseases where matrix metalloproteinases have been implicated, e.g., arthritis and tumor metastasis.

PubMed: 8078901
DOI: 10.1073/pnas.91.18.8447

Experimental method

X-RAY DIFFRACTION (1.8 Å)