Article thumbnail
Location of Repository

Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).

By D Zhang, I Botos, F X Gomis-Rüth, R Doll, C Blood, F G Njoroge, J W Fox, W Bode and E F Meyer


The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC, 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

Topics: Research Article
Year: 1994
DOI identifier: 10.1073/pnas.91.18.8447
OAI identifier:
Provided by: PubMed Central
Sorry, our data provider has not provided any external links therefore we are unable to provide a link to the full text.

Suggested articles

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.