Conformation of receptor adopted upon interaction with virus revealed by site-specific fluorescence quenchers and FRET analysis.
作者： Jürgen Wruss , Philipp D. Pollheimer , Irene Meindl , Annett Reichel , Katrin Schulze
DOI: 10.1021/JA807917T
关键词:
摘要: Human rhinovirus serotype 2 (HRV2) specifically binds to very-low-density lipoprotein receptor (VLDLR). Among the eight extracellular repeats of VLDLR, third module (V3) has highest affinity for virus, and 12 copies genetically engineered concatamer V33333-His6 were found bind per virus particle. In present study, ring formation about each 5-fold symmetry axes on HRV2 was demonstrated by fluorescence resonance energy transfer (FRET) between donor acceptor N- C-terminus, respectively. particular, N-terminus labeled with fluorescein, C-terminus a new quencher which bound His6 tag nanomolar (Kd ∼10−8 M) in presence μM NiCl2.
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