pH-induced conformational change of the influenza M2 protein C-terminal domain

被引：61

作者：

Nguyen, Phuong A. ^{[2
]}

Soto, Cinque S. ^{[1
]}

Polishchuk, Alexei ^{[1
]}

Caputo, Gregory A. ^{[1
]}

Tatko, Chad D. ^{[1
]}

Ma, Chunlong ^{[3
]}

Ohigashi, Yuki ^{[3
]}

Pinto, Lawrence H. ^{[3
]}

DeGrado, William F. ^{[1
]}

Howard, Kathleen P. ^{[2
]}

机构：

[1] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

[2] Swarthmore Coll, Dept Chem & Biochem, Swarthmore, PA 19081 USA

[3] Northwestern Univ, Dept Neurobiol & Physiol, Evanston, IL 60208 USA

来源：

BIOCHEMISTRY | 2008年 / 47卷 / 38期

关键词：

D O I：

10.1021/bi801315m

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites. The reo,ion forms a membrane surface helix at both high and low pH, although the arrangement of the monomers within the tetramer changes with pH. Both electrophysiology and EPR data point to a critical role for residue Lys 49.

引用

页码：9934 / 9936

页数：3

共 50 条

[1] Cholesterol-Dependent Conformational Exchange of the C-Terminal Domain of the Influenza A M2 Protein
Kim, Sangwoo S.
Upshur, Mary Alice
Saotome, Kei
Sahu, Indra D.
McCarrick, Robert M.
Feix, Jimmy B.
Lorigan, Gary A.
Howard, Kathleen P.
BIOCHEMISTRY, 2015, 54 (49) : 7157 - 7167
[2] EPR Spectroscopy of the C-terminal Domain of the M2 Protein from Influenza A Virus
Brown, Emily
Phuong Nguyen
Howard, Kathleen P.
BIOPHYSICAL JOURNAL, 2009, 96 (03) : 432A - 432A
[3] EPR spectroscopy of the C-terminal domain of the M2 protein from influenza a virus
Negrey, Natalie
Nguyen, Phuong
Tatko, Chad
DeGrado, William
Howard, Kathleen
BIOPHYSICAL JOURNAL, 2007, : 74A - 74A
[4] Studies of Conformational Exchange of The C-Terminal Amphipathic Helix of The Influenza A M2 Protein by FRET
Li Jun-Bei
Qiu Xiao-Yan
PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS, 2016, 43 (08) : 796 - 800
[5] NATURE OF THE PH-INDUCED CONFORMATIONAL-CHANGES AND EXPOSURE OF THE C-TERMINAL REGION OF CHROMOGRANIN-A
YOO, SH
FERRETTI, JA
FEBS LETTERS, 1993, 334 (03) : 373 - 377
[6] Exploring the early stages of the pH-induced conformational change of influenza hemagglutinin
Zhou, Yu
Wu, Chao
Zhao, Lifeng
Huang, Niu
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2014, 82 (10) : 2412 - 2428
[7] Analysis of Lanthanide-Induced Conformational Change of the C-Terminal Domain on Centrin
Ya-Qin Zhao
Jun Yan
Li Song
Ya-Nan Feng
Ai-Hua Liang
Bin-Sheng Yang
Journal of Fluorescence, 2012, 22 : 485 - 494
[8] Analysis of Lanthanide-Induced Conformational Change of the C-Terminal Domain on Centrin
Zhao, Ya-Qin
Yan, Jun
Song, Li
Feng, Ya-Nan
Liang, Ai-Hua
Yang, Bin-Sheng
JOURNAL OF FLUORESCENCE, 2012, 22 (01) : 485 - 494
[9] The high stability of cruzipain against pH-induced inactivation is not dependent on its C-terminal domain
Stoka, V
Turk, B
McKerrow, JH
Björk, I
Cazzulo, JJ
Turk, V
FEBS LETTERS, 2000, 469 (01) : 29 - 32
[10] Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly
Kochendoerfer, GG
Salom, D
Lear, JD
Wilk-Orescan, R
Kent, SBH
DeGrado, WF
BIOCHEMISTRY, 1999, 38 (37) : 11905 - 11913

← 1 2 3 4 5 →