通过功能二硫键控制血液蛋白质。
Control of blood proteins by functional disulfide bonds.
机构信息
Lowy Cancer Research Centre and Prince of Wales Clinical School, University of New South Wales, Sydney, NSW, Australia.
出版信息
Blood. 2014 Mar 27;123(13):2000-7. doi: 10.1182/blood-2014-01-549816. Epub 2014 Feb 12.
Abstract
Most proteins in nature are chemically modified after they are made to control how, when, and where they function. The 3 core features of proteins are posttranslationally modified: amino acid side chains can be modified, peptide bonds can be cleaved or isomerized, and disulfide bonds can be cleaved. Cleavage of peptide bonds is a major mechanism of protein control in the circulation, as exemplified by activation of the blood coagulation and complement zymogens. Cleavage of disulfide bonds is emerging as another important mechanism of protein control in the circulation. Recent advances in our understanding of control of soluble blood proteins and blood cell receptors by functional disulfide bonds is discussed as is how these bonds are being identified and studied.
摘要
在自然界中，大多数蛋白质在合成后都会发生化学修饰，以控制其功能的方式、时间和地点。蛋白质的 3 个核心特征是翻译后修饰的：氨基酸侧链可以被修饰，肽键可以被切割或异构化，二硫键可以被切割。肽键的切割是循环中蛋白质控制的主要机制，例如血液凝固和补体酶原的激活。二硫键的切割正成为循环中蛋白质控制的另一个重要机制。本文讨论了我们对功能性二硫键控制可溶性血液蛋白和血细胞受体的理解的最新进展，以及这些键是如何被识别和研究的。
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