CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch.

CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch.
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CA-MMP:一种具有新型半胱氨酸阵列的基质金属蛋白酶,但没有经典的半胱氨酸开关。

DOI:
10.1016/s0014-5793(99)01046-7
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发表时间:
1999
期刊:
影响因子:
3.5
通讯作者:
Pei,D
Pei,D
中科院分区:
生物学3区
文献类型:
--
作者:
Pei,D

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在小鼠中发现了一种基质金属蛋白酶(MMP)样基因,该基因含有一个保守的MMP催化结构域和一个RRRR基序。它缺乏一个经典的半胱氨酸开关,但它具有两个新的基序:半胱氨酸阵列(Cys-X6-Cys-X8-Cys-X10-Cys-X3-Cys-X2-Cys)和一个新的Ig折叠。它被命名为CA-MMP后,独特的半胱氨酸阵列基序,并很少知道它的生化功能。在试图表征CA-MMP活性的过程中,全长序列在哺乳动物细胞中表达,发现其产物与细胞相关而没有可检测的分泌。鉴于这一不寻常的发现,构建了结合CA-MMP的催化结构域与基质分解素-3的前结构域的嵌合体,以在哺乳动物细胞中表达完全活性的酶。纯化的CA-MMP催化结构域以MMP抑制剂敏感的方式表达针对蛋白质底物的蛋白水解活性。两者合计,它的结论是,CA-MMP是一种MMP与不同的结构,生化特性和进化历史,可能会定义一个新的亚类的MMP超家族。
A matrix metalloproteinase (MMP)-like gene was identified in mouse to contain a conserved MMP catalytic domain and an RRRR motif. It lacks a classic cysteine switch, but it possesses two novel motifs: a cysteine array (Cys-X6-Cys-X8-Cys-X10-Cys-X3-Cys-X2-Cys), and a novel Ig-fold. It is named CA-MMP after the distinct cysteine array motif, and little is known about its biochemical function. In an attempt to characterize CA-MMP activity, the full-length sequence was expressed in mammalian cells and its product found to be cell-associated without detectable secretion. In light of this unusual finding, a chimera combining the catalytic domain of CA-MMP with the prodomain of stromelysin-3 was constructed to express a fully active enzyme in mammalian cells. Purified CA-MMP catalytic domain expresses proteolytic activity against protein substrates in an MMP inhibitor sensitive fashion. Taken together, it is concluded that CA-MMP is an MMP with distinct structure, biochemical properties and evolutionary history that may define a new subclass of the MMP superfamily.
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