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. Author manuscript; available in PMC: 2016 Oct 1.
Published in final edited form as: J Biomol Screen. 2015 Jun 4;20(9):1124–1131. doi: 10.1177/1087057115589590

Figure 1. The interaction of TRIP8b and HCN.

Figure 1

A. Schematic showing the interaction between TRIP8b and HCN. Although two interaction sites exist, the downstream interaction between the TPR domains of TRIP8b and the SNL tripeptide of HCN channels is crucial for surface trafficking and function of the channel. B. Coomassie stain showing the full length TRIP8b at left and the shorter TRIP8b(241-602) on the right. Molecular weight markers are indicated on the left. C. Schematic showing the fluorescence polarization assay displayed in (D). D. The fluorescence polarization signal for each concentration of HCN1 peptide is shown. By titrating in increasing quantities of HCN1 peptide labeled with a FITC tag, we observed similar affinities of the two TRIP8b peptides for HCN1.