A distal point mutation in the streptavidin-biotin complex preserves structure but diminishes binding affinity: experimental evidence of electronic polarization effects?
A distal point mutation in the streptavidin-biotin complex preserves structure but diminishes binding affinity: experimental evidence of electronic polarization effects?
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DOI：
10.1021/bi1005392
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发表时间：
2010-06-08
期刊：
影响因子：
2.9
通讯作者：
Lybrand, Terry P.
中科院分区：
文献类型：
--
作者：
Baugh, Loren;Le Trong, Isolde;Cerutti, David S.;Guelich, Susanne;Stayton, Patrick S.;Stenkamp, Ronald E.;Lybrand, Terry P.
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, but all neighboring side chain positions are preserved and protein-biotin hydrogen bonds are unperturbed. Molecular dynamics simulations reveal 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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影响因子：
2.9
作者：
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通讯作者：
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作者：
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DOI：
10.1021/jp9010372
发表时间：
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期刊：
The journal of physical chemistry. B
影响因子：
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发表时间：
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影响因子：
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作者：
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影响因子：
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作者：
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