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Figure 1 | BMC Structural Biology

Figure 1

From: The Host-Pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains

Figure 1

Characterization of the specific interaction of C-terminal Vpr75-90 with CypA and comparison with the interaction with N-terminal binding domain of Vpr. (A) SPR sensorgrams for the specific interaction of synthetic Vpr75-90 with CypA. The peptide was injected at concentrations 0-80 nM over CM5 chip immobilized with CypA to 918 RU. The SPR sensorgrams were fitted to a 1:1 (Langmuir) binding model (black line). (B-C) Comparison of interaction of Vpr75-90 (B) and Vpr30-40 (C) with CypA. The peptides were injected at concentrations ranging from 0-8 μM over CM5 chip immobilized to 180 RU with CypA. (B-C) illustrates the lower affinity of the previously characterized N-terminal binding domain of Vpr [14] to CypA compared with the novel detected C-terminal binding domain.

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