Three-dimensional domain architecture of the ADAM family proteinases.
Three-dimensional domain architecture of the ADAM family proteinases.
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DOI：
10.1016/j.semcdb.2008.07.009
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发表时间：
2009-04
影响因子：
7.3
通讯作者：
S. Takeda
中科院分区：
文献类型：
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作者：
S. Takeda
去整合素和金属蛋白酶（ADAM）蛋白质家族构成哺乳动物膜结合脱落酶的主要类别，其负责细胞表面蛋白质胞外域的加工，包括生长因子、细胞因子及其受体的潜在形式。然而，亚当斯识别和处理其底物的分子机制在很大程度上是未知的。近年来，对蛇毒金属蛋白酶（SVMPs）和哺乳动物血小板反应蛋白1（ADAMTS）家族蛋白的晶体学研究揭示了亚当斯的结构-功能特性。本文将重点介绍这些最近的结构，特别是非催化辅助结构域，这可能是重要的底物识别。
A disintegrin and metalloproteinase (ADAM) family of proteins constitutes a major class of mammalian membrane-bound sheddases that are responsible for the processing of cell-surface-protein ectodomains, including the latent forms of growth factors, cytokines and their receptors. However, the molecular mechanism by which ADAMs recognize and process their substrates is largely unknown. Recent crystallographic studies on phylogenically related snake venom metalloproteinases (SVMPs) and mammalian ADAM with thrombospondin type-1 motif (ADAMTS) family proteins have shed light on the structure-function properties of ADAMs. This review will highlight these recent structures, particularly the non-catalytic ancillary domains, which might be important for substrate recognition.