Preusser A, Briese L, Baur A S, Willbold D
Institut für Molekulare Biotechnologie, D-07745 Jena, Germany.
J Virol. 2001 Apr;75(8):3960-4. doi: 10.1128/JVI.75.8.3960-3964.2001.
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.
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。