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本文引用的文献

1
State-dependent cAMP binding to functioning HCN channels studied by patch-clamp fluorometry.通过膜片钳荧光法研究功能型 HCN 通道的 cAMP 状态依赖性结合。
Biophys J. 2011 Mar 2;100(5):1226-32. doi: 10.1016/j.bpj.2011.01.034.
2
Structural basis for the cAMP-dependent gating in the human HCN4 channel.人类 HCN4 通道中 cAMP 依赖性门控的结构基础。
J Biol Chem. 2010 Nov 19;285(47):37082-91. doi: 10.1074/jbc.M110.152033. Epub 2010 Sep 9.
3
Interdependence of receptor activation and ligand binding in HCN2 pacemaker channels.HCN2 起搏通道中受体激活与配体结合的相互依赖性。
Neuron. 2010 Jul 15;67(1):75-85. doi: 10.1016/j.neuron.2010.05.022.
4
Mapping the structure and conformational movements of proteins with transition metal ion FRET.利用过渡金属离子荧光共振能量转移技术绘制蛋白质的结构和构象变化图谱。
Nat Methods. 2009 Jul;6(7):532-7. doi: 10.1038/nmeth.1341. Epub 2009 Jun 14.
5
Gating of HCN channels by cyclic nucleotides: residue contacts that underlie ligand binding, selectivity, and efficacy.环核苷酸对超极化激活的环核苷酸门控通道的调控：构成配体结合、选择性和效能基础的残基接触。
Structure. 2007 Jun;15(6):655-70. doi: 10.1016/j.str.2007.04.012.
6
Voltage sensor movement and cAMP binding allosterically regulate an inherently voltage-independent closed-open transition in HCN channels.电压传感器的移动和环磷酸腺苷（cAMP）结合通过变构调节超极化激活的环核苷酸门控（HCN）通道中固有的非电压依赖性关闭-开放转变。
J Gen Physiol. 2007 Feb;129(2):175-88. doi: 10.1085/jgp.200609585.
7
Dynamically driven protein allostery.动态驱动的蛋白质别构效应
Nat Struct Mol Biol. 2006 Sep;13(9):831-8. doi: 10.1038/nsmb1132. Epub 2006 Aug 13.
8
cAMP Modulation of the cytoplasmic domain in the HCN2 channel investigated by molecular simulations.通过分子模拟研究HCN2通道中cAMP对细胞质结构域的调节作用。
Biophys J. 2006 May 15;90(10):3428-33. doi: 10.1529/biophysj.105.071621. Epub 2006 Feb 24.
9
Functional expression of the human HCN3 channel.人类HCN3通道的功能表达。
J Biol Chem. 2005 Oct 14;280(41):34635-43. doi: 10.1074/jbc.M502508200. Epub 2005 Jul 25.
10
The murine HCN3 gene encodes a hyperpolarization-activated cation channel with slow kinetics and unique response to cyclic nucleotides.小鼠HCN3基因编码一种超极化激活的阳离子通道，其动力学缓慢，对环核苷酸有独特反应。
J Biol Chem. 2005 Jul 22;280(29):27056-61. doi: 10.1074/jbc.M502696200. Epub 2005 May 27.

环腺苷酸与 HCN 通道 C 末端结合的能量学揭示了负协同性。

Energetics of cyclic AMP binding to HCN channel C terminus reveal negative cooperativity.

机构信息

Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.

Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.

出版信息

J Biol Chem. 2012 Jan 2;287(1):600-606. doi: 10.1074/jbc.M111.269563. Epub 2011 Nov 14.

DOI:10.1074/jbc.M111.269563
PMID:22084239
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3249114/
Abstract

Cyclic AMP binds to the HCN channel C terminus and variably stabilizes its open state. Using isothermal titration calorimetry, we show that cAMP binds to one subunit of tetrameric HCN2 and HCN4 C termini with high affinity (∼0.12 μM) and subsequently with low affinity (∼1 μM) to the remaining three subunits. Changes induced by high affinity binding already exist in both a constrained HCN2 tetramer and the unconstrained HCN1 tetramer. Natural "preactivation" of HCN1 may explain both the smaller effect of cAMP on stabilizing its open state and the opening of unliganded HCN1, which occurs as though already disinhibited.

摘要

环磷酸腺苷与 HCN 通道 C 末端结合，并可使该通道的开放状态发生不同程度的稳定。通过使用等温滴定量热法，我们发现 cAMP 以高亲和力（约 0.12 μM）结合于四聚体 HCN2 和 HCN4 C 末端的一个亚基上，随后以低亲和力（约 1 μM）结合于剩余的三个亚基上。高亲和力结合所诱导的构象变化在受到约束的 HCN2 四聚体和不受约束的 HCN1 四聚体中均已存在。HCN1 的天然“预激活”可能解释了 cAMP 对稳定其开放状态的影响较小，以及未结合配体的 HCN1 也会发生开放的原因，这就好像 HCN1 已经去抑制了一样。