Conformational ensemble of the sodium-coupled aspartate transporter

被引：0
|
作者：
Elka R Georgieva
Peter P Borbat
Christopher Ginter
Jack H Freed
Olga Boudker
机构：
[1] National Biomedical Center for Advanced Electron Spin Resonance Technology,Department of Chemistry and Chemical Biology
[2] Cornell University,Department of Physiology and Biophysics
[3] Cornell University,undefined
[4] Weill Cornell Medical College,undefined
来源：
Nature Structural & Molecular Biology | 2013年 / 20卷
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摘要：
The sodium and aspartate symporter GltPh mediates transport by alternating between outward-facing and inward-facing states. These conformational changes are now probed using double electron-electron resonance (DEER) spectroscopy. The data show that GltPh samples both states with similar probabilities, and that each protomer in the GltPh homotrimer behaves independently of the others.
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页码：215 / 221
页数：6
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