NMR assignments for a helical 40 kDa membrane protein

被引：66

作者：

Oxenoid, K

Kirn, HJ

Jacob, J

Sönnichsen, FD

Sanders, CR ^{[1
]}

机构：

[1] Vanderbilt Univ, Dept Biochem, Nashville, TN 37232 USA

[2] Vanderbilt Univ, Ctr Struct Biol, Nashville, TN 37232 USA

[3] Case Western Reserve Univ, Dept Physiol & Biophys, Cleveland, OH 44106 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 16期

关键词：

D O I：

10.1021/ja049916m

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Backbone nuclear magnetic resonance (NMR) assignments were achieved for diacylglycerol kinase (DAGK) in detergent micelles. DAGK is a homotrimeric integral membrane protein comprised of 121 residue subunits, each having three transmembrane segments. Assignments were made using TROSY-based pulse sequences. DAGK was found to be an almost exclusively helical protein. This work points to the feasibility of both solving the structure of DAGK using solution NMR methods and using NMR as a primary tool in structural studies of other helical integral membrane proteins of similar size and complexity. Copyright © 2003 American Chemical Society.

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页码：5048 / 5049

页数：2

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