The tight interaction between the small molecule biotin and the tetrameric protein streptavidin is widely exploited for many different applications in protein science. In this issue, researchers present the design of a monovalent streptavidin tetramer with a single biotin binding site and demonstrate its enhanced properties over wild-type streptavidin for use in cell-surface protein labeling.
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References
Howarth, M. et al. Nat. Methods 3, 267–273 (2006).
Howarth, M., Takao, K., Hayashi, Y. & Ting, A.Y. Proc. Natl. Acad. Sci. USA 102, 7583–7588 (2005).
Campbell, R.E. et al. Proc. Natl. Acad. Sci. USA 99, 7877–7882 (2002).
George, N., Pick, H., Vogel, H., Johnsson, N. & Johnsson, K. J. Am. Chem. Soc. 126, 8896–8897 (2004).
Yin, J. et al. Proc. Natl. Acad. Sci. USA 102, 15815–15820 (2005).
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Lemercier, G., Johnsson, K. Chimeric streptavidins with reduced valencies. Nat Methods 3, 247–248 (2006). https://doi.org/10.1038/nmeth0406-247
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DOI: https://doi.org/10.1038/nmeth0406-247