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本文引用的文献

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Reduced curvature of ligand-binding domain free-energy surface underlies partial agonism at NMDA receptors.NMDA受体上配体结合域自由能表面曲率降低是部分激动作用的基础。
Structure. 2015 Jan 6;23(1):228-236. doi: 10.1016/j.str.2014.11.012. Epub 2014 Dec 24.
2
Multidimensional reaction rate theory with anisotropic diffusion.具有各向异性扩散的多维反应速率理论
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Structural mechanism of glutamate receptor activation and desensitization.谷氨酸受体激活与脱敏的结构机制。
Nature. 2014 Oct 16;514(7522):328-34. doi: 10.1038/nature13603. Epub 2014 Aug 3.
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Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states.AMPA受体GluA2在静息、预开放和脱敏状态下的结构与动力学
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Structure of an agonist-bound ionotropic glutamate receptor.激动型谷氨酸受体结合态的结构
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6
X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism.AMPA 受体-锥蜗牛毒素复合物的 X 射线结构阐明了其激活机制。
Science. 2014 Aug 29;345(6200):1021-6. doi: 10.1126/science.1258409. Epub 2014 Aug 7.
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Crystal structure of a heterotetrameric NMDA receptor ion channel.NMDA 受体离子通道四聚体的晶体结构。
Science. 2014 May 30;344(6187):992-7. doi: 10.1126/science.1251915.
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Mechanical coupling maintains the fidelity of NMDA receptor-mediated currents.机械偶联维持 NMDA 受体介导电流的保真度。
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9
Conformational analysis of NMDA receptor GluN1, GluN2, and GluN3 ligand-binding domains reveals subtype-specific characteristics.NMDA 受体 GluN1、GluN2 和 GluN3 配体结合域的构象分析揭示了亚型特异性特征。
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10
Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange.氢氘交换实验揭示了完全激动剂和部分激动剂存在下 GluA2 配体结合域裂隙关闭的动力学
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基于机制的离子型谷氨酸受体门控数学模型

Mechanism-Based Mathematical Model for Gating of Ionotropic Glutamate Receptors.

作者信息

Dai Jian, Wollmuth Lonnie P, Zhou Huan-Xiang

机构信息

Department of Physics and Institute of Molecular Biophysics, Florida State University , Tallahassee, Florida 32306, United States.

Department of Neurobiology and Behavior and Center for Nervous System Disorders, Stony Brook University , Stony Brook, New York 11794, United States.

出版信息

J Phys Chem B. 2015 Aug 27;119(34):10934-40. doi: 10.1021/acs.jpcb.5b00521. Epub 2015 Apr 1.

DOI:10.1021/acs.jpcb.5b00521
PMID:25793415
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4552600/
Abstract

We present a mathematical model for ionotropic glutamate receptors (iGluR's) that is built on mechanistic understanding and yields a number of thermodynamic and kinetic properties of channel gating. iGluR's are ligand-gated ion channels responsible for the vast majority of fast excitatory neurotransmission in the central nervous system. The effects of agonist-induced closure of the ligand-binding domain (LBD) are transmitted to the transmembrane channel (TMC) via interdomain linkers. Our model demonstrates that, relative to full agonists, partial agonists may reduce either the degree of LBD closure or the curvature of the LBD free energy basin, leading to less stabilization of the channel open state and hence lower channel open probability. A rigorous relation is derived between the channel closed-to-open free energy difference and the tension within the linker. Finally, by treating LBD closure and TMC opening as diffusive motions, we obtain gating trajectories that resemble stochastic current traces from single-channel recordings and calculate the rate constants for transitions between the channel open and closed states. Our model can be implemented by molecular dynamics simulations to realistically depict iGluR gating and may guide functional experiments in gaining deeper insight into this essential family of channel proteins.

摘要

我们提出了一种基于机制理解构建的离子型谷氨酸受体(iGluR)数学模型,该模型产生了通道门控的许多热力学和动力学特性。iGluR是配体门控离子通道,负责中枢神经系统中绝大多数快速兴奋性神经传递。激动剂诱导的配体结合结构域(LBD)关闭的效应通过结构域间连接子传递到跨膜通道(TMC)。我们的模型表明,相对于完全激动剂,部分激动剂可能会降低LBD关闭的程度或LBD自由能盆地的曲率,导致通道开放状态的稳定性降低,从而降低通道开放概率。推导出通道关闭到开放的自由能差与连接子内张力之间的严格关系。最后,通过将LBD关闭和TMC开放视为扩散运动,我们获得了类似于单通道记录中随机电流轨迹的门控轨迹,并计算了通道开放和关闭状态之间转换的速率常数。我们的模型可以通过分子动力学模拟来实现,以逼真地描绘iGluR门控,并可能指导功能实验,以更深入地了解这个重要的通道蛋白家族。