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1atl
From Proteopedia
| 1atl, resolution 1.80Å () | |||||
|---|---|---|---|---|---|
| Ligands: | , , | ||||
| Non-Standard Residues: | |||||
| Activity: | Atrolysin C, with EC number 3.4.24.42 | ||||
| Domains: | ZnMc_adamalysin_II_like, IBR | ||||
| |||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||
| Coordinates: | save as pdb, mmCIF, xml | ||||
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 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.
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)., Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8447-51. PMID:8078901
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ATL is a Single protein structure of sequence from Crotalus atrox. Full crystallographic information is available from OCA.
Reference
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)., Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8447-51. PMID:8078901
Page seeded by OCA on Mon Jun 30 17:34:12 2008
