ArticleProtein science : a publication of the Protein Society2011
Evolved streptavidin mutants reveal key role of loop residue in high-affinity binding.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 27 citations in OpenAlex.
- Liposomal nanoprobes actuated by engineered water channels for sensitive detection of molecular targets by MRI.Nature biomedical engineering · 2026Article
- Getting the Right Grip? How Understanding Electrophile Selectivity Profiles Could Illuminate Our Understanding of Redox Signaling.Antioxidants & redox signaling · 2020Article
- Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity.Scientific reports · 2020Article
- Functional protein nanostructures: a chemical toolbox.Chemical Society reviews · 2018Review
- Ribonucleoprotein purification and characterization using RNA Mango.RNA (New York, N.Y.) · 2017Article
- Elastin-like polypeptide switches: A design strategy to detect multimeric proteins.Protein science : a publication of the Protein Society · 2017Article
- The Crystal Structure of Monovalent Streptavidin.Scientific reports · 2016Article
- Monovalent streptavidin that senses oligonucleotides.Angewandte Chemie (International ed. in English) · 2013Article
- Decoupling nucleosome recognition from DNA binding dramatically alters the properties of the Chd1 chromatin remodeler.Nucleic acids research · 2013Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We have performed a detailed analysis of streptavidin variants with altered specificity towards desthiobiotin. In addition to changes in key residues which widen the ligand binding pocket and accommodate the more structurally flexible desthiobiotin, the data revealed the role of a key, non-active site mutation at the base of the flexible loop (S52G) which slows dissociation of this ligand by approximately sevenfold. Our data suggest that this mutation results in the loss of a stabilizing contact which keeps this loop open and accessible in the absence of ligand. When this mutation was introduced into the wild-type protein, destabilization of the opened loop conferred a ∼10-fold decrease in both the on-rate and off-rate for the ligand biotin-4-fluoroscein. A similar effect was observed when this mutation was added to a monomeric form of this protein. Our results provide key insight into the role of the streptavidin flexible loop in ligand binding and maintaining high affinity interactions.
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