Structural analysis of CXCR4 - Antagonist interactions using saturation-transfer double-difference NMR
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- 作者：Bryan D. Cox1 ; Anil K. Mehta1 ; John O. DiRaddo ; Dennis C. Liotta ; Lawrence J. Wilson ; James P. Snyder ; jsnyder@emory.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：G-protein-coupled receptors ; NMR spectroscopy ; Saturation transfer difference ; Ligand&ndash ; receptor interactions ; C-X-C chemokine receptor 4
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2015
- 出版时间：9 October 2015
- 年：2015
- 卷：466
- 期：1
- 页码：28-32
- 全文大小：568 K
文摘
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Saturation transfer difference NMR for antagonists bound to the CXCR4 receptor in cellular membrane extracts is presented.
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Competitive binding between two CXCR4 antagonists using STD NMR is established.
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The STD-NMR binding epitope of a small molecule CXCR4 antagonist is identified.
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A 3D model consistent with the experimentally-derived epitope is proposed.