Fig. 1: hRSV NS1 binds hMED25 ACID with high affinity. | Nature Communications

Fig. 1: hRSV NS1 binds hMED25 ACID with high affinity.

From: Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25

Fig. 1

A Domain organization of NS1 and MED25. MED25 contains an N-terminal von Willebrand factor A domain (VWA) and a C-terminal activator interactor domain (ACID). In vitro pulldown assays for B MBP-NS1 with MED25 ACID (left), MBP with MED25 ACID (middle), and GST-MED25 VWA with NS1 (right). M, marker; FB, final beads; E, eluate; W, wash. Data shown is a representative of three independent experiments. C SEC-MALS analysis of the NS1/MED25 ACID complex (black) with a determined molecular weight of 33.7 ± 0.18 kDa compared to NS1 alone (teal) and MED25 ACID alone (violet). Inset, Coomassie stained SDS-PAGE of the protein complex. Data shown is a representative of three independent experiments. D Raw data and binding isotherm for MED25 ACID binding to NS1 measured by ITC. Data shown is a representative of three independent experiments.

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