The structure of the SBP-Tag–streptavidin complex reveals a novel helical scaffold bridging binding pockets on separate subunits

The 38-residue SBP-Tag binds to streptavidin more tightly (K (d) ≃ 2.5–4.9 nM) than most if not all other known peptide sequences. Crystallographic analysis at 1.75 Å resolution shows that the SBP-Tag binds to streptavidin in an unprecedented manner by simultaneously interacting with biotin-binding...

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Hlavní autoři: Barrette-Ng, Isabelle H., Wu, Sau-Ching, Tjia, Wai-Mui, Wong, Sui-Lam, Ng, Kenneth K. S.
Médium: Artigo
Jazyk:Inglês
Vydáno: International Union of Crystallography 2013
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Research Papers
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3640474/
https://ncbi.nlm.nih.gov/pubmed/23633599
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S0907444913002576
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