Diverse Pathways of Oxidative Folding of Disulfide Proteins: Underlying Causes and Folding Models
Diverse Pathways of Oxidative Folding of Disulfide Proteins: Underlying Causes and Folding Models
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DOI：
10.1021/bi200131j
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发表时间：
2011-05-03
期刊：
影响因子：
2.9
通讯作者：
Chang, Jui-Yoa
中科院分区：
文献类型：
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作者：
Chang, Jui-Yoa
二硫键蛋白的氧化折叠途径具有高度的多样性，主要表现为明显的结构异质性和折叠中间体的多种重排途径。在过去的二十年中，通过各种实验室对30多种富含二硫化物的蛋白质的研究，这种多样性的范围已经扩大。一个更全面的景观蛋白质氧化折叠的机制已经出现。这次审查将涉及三个主题。(1)二硫键折叠途径的多样性范围，包括以牛胰胰蛋白酶抑制剂（BPTI）和水蛭素为代表的两种相反的极端模式。(2)解释折叠多样性的潜在机制的实验证据的证明。(3)讨论氧化折叠的极端模型与传统构象折叠模型（框架模型、疏水折叠模型）之间的趋同性。
The pathway of oxidative folding of disulfide proteins exhibits a high degree of diversity, which is manifested mainly by distinct structural heterogeneity and diverse rearrangement pathways of folding intermediates. During the past two decades, the scope of this diversity has widened through studies of more than 30 disulfide-rich proteins by various laboratories. A more comprehensive landscape of the mechanism of protein oxidative folding has emerged. This review will cover three themes. (1) Elaboration of the scope of diversity of disulfide folding pathways, including the two opposite extreme models, represented by bovine pancreatic trypsin inhibitor (BPTI) and hirudin. (2) Demonstration of experimental evidence accounting for the underlying mechanism of the folding diversity. (3) Discussion of the convergence between the extreme models of oxidative folding and models of conventional conformational folding (framework model, hydrophobic collapse model).