Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form d)

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 wit...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1994-08, Vol.91 (18), p.8447-8451
Hauptverfasser:	Zhang, Dachuan, Botos, Istvan, Gomis-Rüth, Franz-Xaver, Doll, Ronald, Blood, Christine, Njoroge, F. George, Fox, Jay w., Bode, Wolfram, Meyer, Edgar F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Active sites Amides - pharmacology Amino Acid Sequence Atoms Binding Sites Biochemistry Collagens Crotalid Venoms Crotalus atrox Crystallography, X-Ray Disease Enzymes Ligands Metalloendopeptidases - antagonists & inhibitors Models, Molecular Molecular Sequence Data Molecules Poisons Protein Structure, Tertiary Snakes Tyrosine - analogs & derivatives Tyrosine - pharmacology Venoms Zinc
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Zusammenfassung:	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 (
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.91.18.8447