Catalytic domain of MMP20 (Enamelysin) - The NMR structure of a new matrix metalloproteinase
Catalytic domain of MMP20 (Enamelysin) - The NMR structure of a new matrix metalloproteinase
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DOI：
10.1016/j.febslet.2007.08.069
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发表时间：
2007-10-02
期刊：
影响因子：
3.5
通讯作者：
Gonnelli, Leonardo
中科院分区：
文献类型：
--
作者：
Arendt, Yvonne;Banci, Lucia;Gonnelli, Leonardo
MMP-20的催化结构域的解决方案的结构，尚未结构特征的基质金属蛋白酶家族的成员，与N-异丁基-N-（4-甲氧苯磺酰基）甘氨酰异羟肟酸（NNGH）的络合物，在这里报道和比较与其他MMPs-NNGH加合物。骨架动力学也已被表征。我们已经发现，尽管相同的折叠和非常高的整体相似性，本结构经历了特定的结构和动力学的相似性与一些MMP和差异与其他人，周围的催化腔。本发明的溶液结构不仅有助于填补关于人MMP的结构知识的差距，而且还提供了进一步的信息，以设计针对这类蛋白质的特定成员的更具选择性和有效的抑制剂。(c)2007年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.