This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1htd
From Proteopedia
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Atrolysin C, with EC number 3.4.24.42 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)
Overview
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.
About this Structure
1HTD 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 Sun Mar 30 21:10:10 2008
