Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
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天然和合成抑制剂与毒液金属蛋白酶 Atrolysin C（形式 d）的结构相互作用。
DOI：
10.1073/pnas.91.18.8447
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发表时间：
1994
影响因子：
11.1
通讯作者：
Meyer,EF
中科院分区：
文献类型：
--
作者：
Zhang,D;Botos,I;Gomis-Rüth,FX;Doll,R;Blood,C;Njoroge,FG;Fox,JW;Bode,W;Meyer,EF
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.
