Solution-state NMR spectroscopy of a seven-helix transmembrane protein receptor: Backbone assignment, secondary structure, and dynamics

被引：47

作者：

Gautier, Antoine ^{[1
]}

Kirkpatrick, John P. ^{[1
]}

Nietlispach, Daniel ^{[1
]}

机构：

[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 38期

基金：

英国生物技术与生命科学研究理事会;

关键词：

membrane proteins; NMR spectroscopy; protein structures; receptors; structure elucidation;

D O I：

10.1002/anie.200802783

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Protein in motion: A solution-state NMR study on the seven-helix transmembrane protein pSRII (see picture) in a detergent solution focused on the sequential backbone assignment, the characterization of the secondary structure, and the backbone dynamics. The structural integrity of the protein was confirmed, and mobility in the loops (ps-ns timescale) and slower motions in the helical core (ms-ms timescale) were identified. (Figure Presented) © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

收藏

页码：7297 / 7300

页数：4

相关论文

共 28 条

[1]

[Anonymous], 2007, ANGEW CHEM, V119, P463

[2] Conformational dynamics of the KcsA potassium channel governs gating properties [J].

Baker, Kent A. ;

Tzitzilonis, Christos ;

Kwiatkowski, Witek ;

Choe, Senyon ;

Riek, Roland .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2007, 14 (11) :1089-1095

[3] CONVENTIONAL AND EXPONENTIAL SAMPLING FOR 2D NMR EXPERIMENTS WITH APPLICATION TO A 2D NMR-SPECTRUM OF A PROTEIN [J].

BARNA, JCJ ;

LAUE, ED .

JOURNAL OF MAGNETIC RESONANCE, 1987, 75 (02) :384-389

[4] Temperature dependence of H-1 chemical shifts in proteins [J].

Baxter, NJ ;

Williamson, MP .

JOURNAL OF BIOMOLECULAR NMR, 1997, 9 (04) :359-369

[5] The structure of the ζζ transmembrane dimer reveals features essential for its assembly with the T cell receptor [J].

Call, Matthew E. ;

Schnell, Jason R. ;

Xu, Chenqi ;

Lutz, Regina A. ;

Chou, James J. ;

Wucherpfennig, Kai W. .

CELL, 2006, 127 (02) :355-368

[6] NMR study of the tetrameric KcsA potassium channel in detergent micelles [J].

Chill, JH ;

Louis, JM ;

Miller, C ;

Bax, A .

PROTEIN SCIENCE, 2006, 15 (04) :684-698

[7] Modulation of folding and assembly of the membrane protein bacteriorhodopsin by intermolecular forces within the lipid bilayer [J].

Curran, AR ;

Templer, RH ;

Booth, PJ .

BIOCHEMISTRY, 1999, 38 (29) :9328-9336

[8] Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy [J].

Etzkorn, Manuel ;

Martell, Swetlana ;

Andronesi, Ovidiu C. ;

Seidel, Karsten ;

Engelhard, Martin ;

Baldus, Marc .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2007, 46 (03) :459-462

[9] Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase [J].

Girvin, ME ;

Rastogi, VK ;

Abildgaard, F ;

Markley, JL ;

Fillingame, RH .

BIOCHEMISTRY, 1998, 37 (25) :8817-8824

[10] NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system [J].

Howell, SC ;

Mesleh, MF ;

Opella, SJ .

BIOCHEMISTRY, 2005, 44 (13) :5196-5206