Identification of Three Interactions to Determine the Conformation Change and to Maintain the Function of Kir2.1 Channel Protein

doi:10.1088/0256-307X/32/2/028702

Chin. Phys. Lett.

2015, Vol. 32

Issue (02): 028702 DOI: 10.1088/0256-307X/32/2/028702

CROSS-DISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY

Identification of Three Interactions to Determine the Conformation Change and to Maintain the Function of Kir2.1 Channel Protein

LI Jun-Wei¹, XIAO Shao-Ying², XIE Xiao-Xiao¹, YU Hui¹, ZHANG Hai-Lin³, ZHAN Yong^1**, AN Hai-Long^1**

¹Key Laboratory of Molecular Biophysics of Hebei Province, Institute of Biophysics, School of Sciences, Hebei University of Technology, Tianjin 300401
²School of Architecture & Art Design, Hebei University of Technology, Tianjin 300401
³Key Laboratory of Neural and Vascular Biology (Ministry of Education), The Key Laboratory of Pharmacology and Toxicology for New Drug of Hebei Province, Department of Pharmacology, Hebei Medical University, Shijiazhuang 050017

Cite this article:

LI Jun-Wei, XIAO Shao-Ying, XIE Xiao-Xiao et al 2015 Chin. Phys. Lett. 32 028702

Download: PDF(980KB)
Export: BibTeX | EndNote | Reference Manager | ProCite | RefWorks

Abstract We find that a conserved mutation residue Glu to residue Asp (E303D), which both have the same polar and charged properties, makes Kir2.1 protein lose its function. To understand the mechanism, we identify three interactions which control the conformation change and maintain the function of the Kir2.1 protein by combining homology modeling and molecular dynamics with targeted molecular dynamics. We find that the E303D mutation weakens these interactions and results in the loss of the related function. Our data indicate that not only the amino residues but also the interactions determine the function of proteins.

Published: 20 January 2015

PACS:	87.15.hp	(Conformational changes)
	87.15.ap	(Molecular dynamics simulation)
	87.16.Vy	(Ion channels)

TRENDMD:

URL:

https://cpl.iphy.ac.cn/10.1088/0256-307X/32/2/028702 OR https://cpl.iphy.ac.cn/Y2015/V32/I02/028702

Service
	E-mail this article
	E-mail Alert
	RSS
Articles by authors
	LI Jun-Wei
	XIAO Shao-Ying
	XIE Xiao-Xiao
	YU Hui
	ZHANG Hai-Lin
	ZHAN Yong
	AN Hai-Long

[1] Decher N et al 2007 Cardiovasc. Res. 75 748
[2] An H L et al 2012 J. Biol. Chem. 287 42278
[3] Rezazadeh S et al 2010 Biophys. J. 98 120a
[4] Hansen S B et al 2011 Nature 477 495
[5] Hibino H et al 2010 Physiol. Rev. 90 291
[6] Logothetis D E et al 2007 Pflügers Arch. 455 83
[7] Pegan S et al 2005 Nat. Neurosci. 8 279
[8] Bavro V N et al 2012 Nat. Struct. Mol. Biol. 19 158
[9] Kubo Y et al 1993 Nature 364 802
[10] Makhina E N et al 1994 J. Biol. Chem. 269 20468
[11] Donaldson M R et al 2003 Neurology 60 1811
[12] Li J W et al 2014 Sci. Rep. (Submitted)
[13] Yu T et al 2014 Chin. Phys. Lett. 31 068701
[14] Geng Y Z et al 2014 Chin. Phys. Lett. 31 048702
[15] Schlitter J, Engels M and Kruger P 1994 J. Mol. Graphics 12 84
[16] Guex N and Peitsch M C 1997 Electrophoresis 18 2714
[17] Schwede T et al 2003 Nucl. Acids Res. 31 3381
[18] Arnold K et al 2006 Bioinformatics 22 195
[19] Humphrey W, Dalke A and Schulten K 1996 J. Mol. Graphics 14 33
[20] Cheng X et al 2006 PLoS Comput. Biol. 2 e134
[21] Phillips J C et al 2005 J. Comput. Chem. 26 1781
[22] MacKerell A D et al 1998 J. Phys. Chem. B 102 3586
[23] Feller S E et al 1995 J. Chem. Phys. 103 4613
[24] Essmann U et al 1995 J. Chem. Phys. 103 8577
[25] Lopes C M et al 2002 Neuron 34 933

Related articles from Frontiers Journals

[1]	Qian-Yun Liang, Chun-Li Pang, Jun-Wei Li, Su-Hua Zhang, Hui Liu, Yong Zhan, Hai-Long An. Allosteric Mechanism of Calmodulin Revealed by Targeted Molecular Dynamics Simulation[J]. Chin. Phys. Lett., 2017, 34(6): 028702
[2]	Yi-Zhao Geng, Hui Zhang, Gang Lyu, Qing Ji. Initiation Mechanism of Kinesin's Neck Linker Docking Process[J]. Chin. Phys. Lett., 2017, 34(2): 028702
[3]	Xiao-Xiao Xie, Jun-Wei Li, Shao-Ying Xiao, Yu-Zhi Liu, Hui Liu, Jin-Peng Geng, Su-Hua Zhang, Hui Yu, Yong Zhan, Hai-Long An. The Structural Stability of Alpha-Helix Determined by the Preference of Amino Acids[J]. Chin. Phys. Lett., 2016, 33(02): 028702
[4]	GENG Yi-Zhao, ZHANG Hui, JI Qing, YAN Shi-Wei. Locking Function of a Key Residue in Kinesin's Gating Mechanism[J]. Chin. Phys. Lett., 2014, 31(04): 028702
[5]	GU Fang, WANG Hai-Jun, HONG Xiao-Zhong, BA Xin-Wu. Translocation of Biopolymer Chain Through a Nanopore: Coil--Helix Transition[J]. Chin. Phys. Lett., 2008, 25(8): 028702

Viewed

Full text

Abstract