Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites

Jeon, B.J.; Kim, S.; Kim, M.-S.; Lee, J.-H.; Kim, B.S.; Hwang, K.Y.

doi:10.1107/S2052252520015675

Figure 6
Direct interactions between fluorescently labeled streptavidins and biotin or labeled C-terminal deletion mutants and ligands measured by microscale thermophoresis (MST). (a) Dose–response curves of streptavidin C1 (green), streptavidin C2 (red) or streptavidin (blue) and the biotin molecule. (b) Dose–response curves of ΔC1 + C-Lid_ECP (green), ΔC2 + C-Lid_ECP (blue), ΔC1 + ECP (orange) and ΔC2 + ECP (red). The amino-acid sequences of C-Lid_ECP and ECP were designed as –¹⁶⁹SAADVEKARQLGVTSANPPASDGE¹⁹¹– and –¹⁷⁸LGVTSANPPASDGE¹⁹¹–, respectively.

IUCrJ

Volume 8| Part 2| March 2021| Pages 168-177

ISSN: 2052-2525

https://doi.org/10.1107/S2052252520015675

BIOLOGY | MEDICINE

Open

access

Follow IUCrJ

Search IUCr Journals		doi		Advanced search
Author		volume	page