The Native Conformation of the Human VDAC1 N Terminus

被引：48

作者：

Schneider, Robert ^{[1
]}

Etzkorn, Manuel ^{[3
]}

Giller, Karin ^{[1
]}

Daebel, Venita ^{[1
]}

Eisfeld, Joerg ^{[2
]}

Zweckstetter, Markus ^{[1
]}

Griesinger, Christian ^{[1
]}

Becker, Stefan ^{[1
]}

Lange, Adam ^{[1
]}

机构：

[1] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077 Gottingen, Germany

[2] Ionovat GmbH, D-49084 Osnabruck, Germany

[3] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 10期

关键词：

ion channels; membrane proteins; NMR spectroscopy; protein structures; DEPENDENT ANION CHANNEL; SOLID-STATE NMR; VOLTAGE; EXPRESSION; RESONANCE; PROTEINS; SEQUENCE;

D O I：

10.1002/anie.200906241

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Roll out the barrel: The conformation of the N-terminal domain of a functional human voltage-dependent anion channel (hVDACl) in lipid bilayers has been determined (see picture; overlay of NMR model (blue) and X-ray structure (red/ gray)). Solid-state NMR spectroscopy reveals that the N terminus assumes a well-defined, rigid structure and that its removal induces a conformational change in the hVDACl β-barrel. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：1882 / 1885

页数：4

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