Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Daizhou ZhangDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843Istvan BotosDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843F. Xavier Gomis‐RüthDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843Ronald J. DollDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843C H BloodDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843F. George NjorogeDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843Jay W. FoxDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843Wolfram BodeDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843E. F. MeyerDepartment of Biochemistry and Biophysics, Texas A&M University, College Station 77843
1994en
ABI
Аннотация
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.
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