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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Inverting the selectivity of aquaporin 6: Gating versus direct electrostatic interaction
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Inverting the selectivity of aquaporin 6: Gating versus direct electrostatic interaction

机译：反转水通道蛋白6的选择性：门控与直接静电相互作用

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摘要

Specialized transmembrane proteins form channels that facilitate the transport of ions and other molecules across the membranes and thus play crucial role in many life processes. The understanding of these systems has increased enormously in recent years because of advances in structural and biochemical studies (e.g., refs. 1 and 2). However, key questions remain with regards to the exact factors that control the selectivity and gating of ion transport across membranes. To understand these factors, it would very useful to quantify the energy contributions that allow some ions to permeate while blocking others, and thus allow channels to fulfill their specific physiological functions. Although the availability of structural information paved the way for detailed scrutiny of different hypotheses and models, there is still a clear need for well defined experimental test cases. In this issue of PNAS, a study of aquaporin 6 (AQP6) by Liu et al. (3) provides a crucial test case in which a mutation of a single residue (a change of Asn-60 to Gly) completely changes the conductance, converting AQP6 from an anion channel to a water-selective channel. This finding provides extremely valuable information whose full "translation" to a functional model probably will require more structural information as well as the use of computer modeling approaches.
机译：专门的跨膜蛋白形成促进离子和其他分子跨膜运输的通道，因此在许多生命过程中都起着至关重要的作用。近年来，由于结构和生化研究的进展（例如，参考文献1和2），对这些系统的了解已大大增加。但是，关键问题仍然是控制离子跨膜传输的选择性和门控性的确切因素。为了理解这些因素，量化允许某些离子渗透而阻止其他离子渗透并因此使通道完成其特定生理功能的能量贡献将非常有用。尽管结构信息的可获得性为详细审查不同假设和模型铺平了道路，但仍然明确需要明确定义的实验测试用例。在本期PNAS中，Liu等人研究了水通道蛋白6（AQP6）。 （3）提供了一个至关重要的测试案例，其中单个残基的突变（从Asn-60变为Gly）完全改变了电导率，将AQP6从阴离子通道转换为水选择性通道。这一发现提供了非常有价值的信息，其对功能模型的完整“翻译”可能需要更多的结构信息以及使用计算机建模方法。

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