Structural and functional diversity of lysyl oxidase and the LOX-like proteins
Structural and functional diversity of lysyl oxidase and the LOX-like proteins
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DOI：
10.1016/s1570-9639(03)00053-0
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发表时间：
2003-04-11
影响因子：
3.2
通讯作者：
Csiszar, K
中科院分区：
文献类型：
--
作者：
Molnar, J;Fong, KSK;Csiszar, K
赖氨酰氧化酶（LOX）和四种赖氨酰氧化酶样蛋白，L0 XL、L0 XL 2、L0 XL 3和L0 XL 4，各自含有铜结合位点、可能有助于醌辅因子形成的保守赖氨酰和酪氨酰残基以及细胞因子受体样结构域。每种蛋白质的不同之处主要在于它们的N-末端序列，这可能赋予个体功能。通过BMP-1和可能的其他机制加工LOX蛋白可能导致多种功能形式。据报道，LOXL 3的剪接也可能产生具有独特功能的其他变体。每种LOX都具有其个体的、发育调节的组织和细胞特异性表达和定位，导致LOX胺氧化酶的复杂结构和功能变异。果蝇中只有两种LOX样蛋白，每种蛋白都具有不同的空间和时间表达，这使得将个体功能分配给这些胺氧化酶中的一种。每个LOX蛋白的比较表达分析，以帮助确定其功能的意义。(C)2003 Elsevier Science B. V.保留所有权利。
Lysyl oxidase (LOX) and four lysyl oxidase-like proteins, LOXL, LOXL2, LOXL3 and LOXL4, each contain a copper binding site, conserved lysyl and tyrosyl residues that may contribute to quinone co-factor formation, and a cytokine receptor-like domain. Each protein differs mainly in their N-terminal sequence, which may confer individual functions. Processing of the LOX proteins by BMP-1 and possibly other mechanisms may result in multiple functional forms. Splicing, reported for LOXL3, may also generate additional variants with unique functions. Each LOX, with its individual, developmentally regulated tissue and cell-specific expression and localization, results in a complex structural and functional variation for the LOX amine oxidases. The presence of only two LOX-like proteins in Drosophila, each with distinct spatial and temporal expression, allows for the assignment of individual function to one of these amine oxidases. Comparative expression analysis of each LOX protein is presented to help determine their functional significance. (C) 2003 Elsevier Science B.V. All rights reserved.