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全长人类免疫缺陷病毒1型Nef蛋白与CD4胞质结构域的直接体外结合

Direct in vitro binding of full-length human immunodeficiency virus type 1 Nef protein to CD4 cytoplasmic domain.

作者信息

Preusser A, Briese L, Baur A S, Willbold D

机构信息

Institut für Molekulare Biotechnologie, D-07745 Jena, Germany.

出版信息

J Virol. 2001 Apr;75(8):3960-4. doi: 10.1128/JVI.75.8.3960-3964.2001.

Abstract

The Nef protein of the simian and human immunodeficiency viruses is known to directly bind and downregulate the CD4 receptor. Although the molecular mechanism is well understood, direct binding of Nef and CD4 is difficult to demonstrate and is believed to be of low affinity. Applying nuclear magnetic resonance and fluorescence spectroscopy, we biophysically reevaluated the CD4-Nef complex and found the dissociation constant to be in the submicromolar range. We conclude that additional, so far disregarded residues in the N terminus of Nef are important for interaction with CD4.

摘要

已知猿猴免疫缺陷病毒和人类免疫缺陷病毒的Nef蛋白可直接结合并下调CD4受体。尽管其分子机制已为人熟知,但Nef与CD4的直接结合难以证实,且被认为亲和力较低。应用核磁共振和荧光光谱技术,我们对CD4-Nef复合物进行了生物物理重新评估,发现其解离常数处于亚微摩尔范围内。我们得出结论,Nef N端中迄今被忽视的其他残基对于与CD4的相互作用很重要。

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本文引用的文献

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Solution Structure of the Human CD4 (403-419) Receptor Peptide.
J Biomed Sci. 1996 Nov-Dec;3(6):435-441. doi: 10.1007/BF02258047.
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