N-hydroxyurea as zinc binding group in matrix metalloproteinase inhibition:: Mode of binding in a complex with MMP-8
N-hydroxyurea as zinc binding group in matrix metalloproteinase inhibition:: Mode of binding in a complex with MMP-8
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DOI：
10.1016/j.bmcl.2005.09.057
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发表时间：
2006-01-01
影响因子：
2.7
通讯作者：
Gallina, C
中科院分区：
文献类型：
--
作者：
Campestre, C;Agamennone, M;Gallina, C
本文报道了结合到基质金属蛋白酶活性位点的N-羟基脲抑制剂的第一个晶体结构。制备了配体和三种其他类似物，并将其作为MMP-2、MMP-3和MMP-8的抑制剂进行研究。与MMP-8的复合物的晶体结构表明，与类似的异羟肟酸盐相反，N-羟基脲以单齿而不是双齿模式结合催化锌离子，并且酰胺键具有高的面外畸变。(c)2005爱思唯尔有限公司保留所有权利。
The first crystallographic structure of an N-hydroxyurea inhibitor bound into the active site of a matrix metalloproteinase is reported. The ligand and three other analogues were prepared and studied as inhibitors of MMP-2, MMP-3, and MMP-8. The crystal structure of the complex with MMP-8 shows that the N-hydroxyurea, contrary to the analogous hydroxamate, binds the catalytic zinc ion in a monodentate rather than bidentate mode and with high out-of-plane distortion of the amide bonds. (c) 2005 Elsevier Ltd. All rights reserved.