The NTR module:: Domains of netrins, secreted frizzled related proteins, and type I procollagen C-proteinase enhancer protein are homologous with tissue inhibitors of metalloproteases
The NTR module:: Domains of netrins, secreted frizzled related proteins, and type I procollagen C-proteinase enhancer protein are homologous with tissue inhibitors of metalloproteases
复制标题
NTR模块：netrins、分泌型frizzled相关蛋白和I型胶原蛋白C蛋白酶增强蛋白的结构域与金属蛋白酶组织抑制剂同源
DOI：
10.1110/ps.8.8.1636
复制
发表时间：
1999-08-01
期刊：
影响因子：
8
通讯作者：
Patthy, L
中科院分区：
文献类型：
--
作者：
Bányai, L;Patthy, L
使用同源性搜索、结构预测和结构表征方法，我们发现 (1) netrins、(2) 补体蛋白 C3、C4、C5、(3) 分泌型卷曲相关蛋白和 (4) I 型前胶原 C 蛋白酶增强蛋白 (PCOLCE) 的 C 端结构域与 (5) 组织抑制剂的 N 端结构域同源。 金属蛋白酶（TIMP）。含有该 netrin 模块（NTR 模块）的蛋白质发挥着多种生物学作用，从轴突引导、Wnt 信号传导调节到金属蛋白酶活性控制。 TIMP 除外。目前尚不清楚 NTR 模块在这些过程中发挥什么作用。鉴于 TIMP 的 NTR 模块参与对基质蛋白型金属蛋白酶的抑制，并且 PCOLCE 的 NTR 模块参与控制虾红素型金属蛋白酶 BMP1 的活性，因此与 metzincins 的相互作用似乎可能是 NTR 模块的共同特性，并且可能对宿主蛋白的生物学作用至关重要。
Using homology search, structure prediction, and structural characterization methods we show that the C-terminal domains of (1) netrins, (2) complement proteins C3, C4, C5, (3) secreted frizzled-related proteins, and (4) type I procollagen C-proteinase enhancer proteins (PCOLCEs) are homologous with the N-terminal domains of (5) tissue inhibitors of metalloproteinases (TIMPs). The proteins harboring this netrin module (NTR module) fulfill diverse biological roles ranging from axon guidance, regulation of Wnt signaling, to the control of the activity of metalloproteases. With the exception of TIMPs. it is not known at present what role the NTR modules play in these processes. In view of the fact that the NTR modules of TIMPs are involved in the inhibition of matrixin-type metalloproteases and that the NTR module of PCOLCEs is involved in the control of the activity of the astacin-type metalloprotease BMP1, it seems possible that interaction with metzincins could be a shared property of NTR modules and could be critical for the biological roles of the host proteins.