ZFIN Image: Bobone et al., 2021, Fig. 5

Image

Figure Caption

Fig. 5

Binding selectivity of Cy3-P9W5 for an array of SH2 domains. In the left panels, the fluorescently labeled analogue Cy3-P9W5 was allowed to interact with an array of human SH2 domains, expressed and purified as glutathione S-transferase (GST) fusion constructs. Binding affinity was assessed by the fluorescence of the bound peptide, at concentrations of 0.5 nM (top), 5.0 nM (center), and 50 nM (bottom). Each SH2 domain was spotted in duplicate, and negative control spots (with GST only) are also present. The bright spots correspond to the N-SH2 domain of SHP2 (circled in red) and to the SH2 domain of the SH2 and PH domain-containing adapter protein APS (also called SHP2B2, circled in yellow). The intensity of all other spots is comparable to that of the negative controls. The right panels shows a control of the protein loading in each spot, performed with an anti-GST antibody (top), and the position of each SH2 domain in the array (bottom). For each SH2 domain, the gene name and Uniprot codes are reported. Each domain was spotted in duplicate.

Acknowledgments

This image is the copyrighted work of the attributed author or publisher, and ZFIN has permission only to display this image to its users. Additional permissions should be obtained from the applicable author or publisher of the image. Full text @ J. Med. Chem.