2 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode
2 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode
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DOI：
10.1016/s0014-5793(97)01401-4
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发表时间：
1997-12-01
期刊：
影响因子：
3.5
通讯作者：
Politi, V
中科院分区：
文献类型：
--
作者：
Cirilli, M;Gallina, C;Politi, V
寻找replysin抑制剂提供了可能性的干预，对matrixins和亚当斯。本文报道了一种内源性蛇毒三肽磷酸盐抑制剂与replysin家族成员adamalysin Ⅱ形成的复合物的晶体结构。该抑制剂以反向结合方式占据切割位点的启动区，磷酸盐基团以不对称双齿方式与锌离子连接，相邻的Trp吲哚系统部分填充初级特异性亚位点S-1 '。肿瘤坏死因子-α-转化酶（TACE）的基于金刚烷的模型揭示了该酶的较小的S-1'口袋。(C)1997年欧洲生物化学学会联合会。
The search of reprolysin inhibitors offers the possibility of intervention against both matrixins and ADAMs. Here we report the crystal structure of the complex between adamalysin II, a member of the reprolysin family, and a phosphonate inhibitor modeled on an endogenous venom tripeptide, The inhibitor occupies the primed region of the cleavage site adopting a retro-binding mode, The phosphonate group ligates the zinc ion in an asymmetric bidentate mode and the adjacent Trp indole system partly fills the primary specificity subsite S-1'. An adamalysin-based model of tumor necrosis factor-alpha-converting enzyme (TACE) reveals a smaller S-1' pocket for this enzyme. (C) 1997 Federation of European Biochemical Societies.