ArticleBiochemistry2010
A distal point mutation in the streptavidin-biotin complex preserves structure but diminishes binding affinity: experimental evidence of electronic polarization effects?
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Molecular dynamics reveal potential effects of novel VHL variants on VHL-Elongin C binding in ccRCC patients from Eastern India.Scientific reports · 2025Article
- Production of mutant streptavidin protein and investigation of its effect on the performance of streptavidin.Iranian journal of basic medical sciences · 2023Article
- A Streptavidin Binding Site Mutation Yields an Unexpected Result: An Ionized Asp128 Residue Is Not Essential for Strong Biotin Binding.Biochemistry · 2016Article
- Classical electrostatics for biomolecular simulations.Chemical reviews · 2014Review
- Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidin.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Second-contact shell mutation diminishes streptavidin-biotin binding affinity through transmitted effects on equilibrium dynamics.Biochemistry · 2012Article
- A continuous fluorescence displacement assay for BioA: an enzyme involved in biotin biosynthesis.Analytical biochemistry · 2011Article
- Streptavidin and its biotin complex at atomic resolution.Acta crystallographica. Section D, Biological crystallography · 2011Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
We have identified a distal point mutation in streptavidin that causes a 1000-fold reduction in biotin binding affinity without disrupting the equilibrium complex structure. The F130L mutation creates a small cavity occupied by a water molecule; however, all neighboring side chain positions are preserved, and protein-biotin hydrogen bonds are unperturbed. Molecular dynamics simulations reveal a reduced mobility of biotin binding residues but no observable destabilization of protein-ligand interactions. Our combined structural and computational studies suggest that the additional water molecule may affect binding affinity through an electronic polarization effect that impacts the highly cooperative hydrogen bonding network in the biotin binding pocket.
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Registered trials
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