Batimastat, a potent matrix metalloproteinase inhibitor, exhibits an unexpected mode of binding

Istvan Botos; Leonardo Scapozza; Dachuan Zhang

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Batimastat, a potent matrix metalloproteinase inhibitor, exhibits an unexpected mode of binding

机译：Batimastat，一种有效的基质金属蛋白酶抑制剂，表现出意想不到的结合方式

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Matrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metal- loproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-A deg resolution (R = 16.8/100). The title structure exhibits an unex- pected binding geometry, with the thiophene ring deeply inserted into the primary specificity site.

机译：基质金属蛋白酶已经参与了退化过程，例如肿瘤细胞的侵袭，转移和关节炎。特定的金属蛋白酶抑制剂已被用于阻断肿瘤细胞的增殖。我们已经检查了巴马司他（BB-94）与金属蛋白酶[atrolysin C（Ht-d），EC 3.4.24.42]活性位点在2.0-A度分辨率下的相互作用（R = 16.8 / 100）。标题结构表现出意外的结合几何形状，噻吩环深深插入一级特异性位点。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1996年第7期|p.2749-2754|共6页
作者
Istvan Botos; Leonardo Scapozza; Dachuan Zhang;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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机译：在小鼠急性肺损伤期间，抗纤维化化合物吡非尼酮和基质金属蛋白酶抑制剂巴马司他对气道重塑相关介质的调节。
2. Synthetic inhibitor of matrix metalloproteinases (batimastat) reduces prostate cancer growth in an orthotopic rat model. [J] . Lein M, Jung K, Le DK, The Prostate . 2000,第2期

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5. Briciclib (on 013105), an elF4E inhibitor, exhibits potent anti-cancer activity in various preclinical cancer models. [D] . Desai, Bina. 2015

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6. Batimastat a potent matrix mealloproteinase inhibitor exhibits an unexpected mode of binding. [O] . I Botos, L Scapozza, D Zhang, 1996

机译：Batimastat（一种有效的基质磷酸蛋白酶抑制剂）表现出出乎意料的结合方式。
7. Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding. [O] . Botos, I, Scapozza, L, Zhang, D, 1996

机译：Batimastat（一种有效的基质磷酸蛋白酶抑制剂）表现出出乎意料的结合方式。

Batimastat, a potent matrix metalloproteinase inhibitor, exhibits an unexpected mode of binding

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