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NMR structure and dynamics of the engineered fluorescein-binding lipocalin FluA reveal rigidification of beta-barrel and variable loops upon enthalpy-driven ligand binding.

Mills JL, Liu G, Skerra A, Szyperski T,
Biochemistry (2009) 48:7411-9 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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The NMR structure of the 21 kDa lipocalin FluA, which was previously obtained by combinatorial design, elucidates a reshaped binding site specific for the dye fluorescein resulting from 21 side chain replacements with respect to the parental lipocalin, the naturally occurring bilin-binding protein (BBP). ...
metabolism chemistry 
Protein Structure, Tertiary Protein Binding Protein Structure, Secondary Recombinant Proteins Ligands Magnetic Resonance Spectroscopy Thermodynamics Protein Engineering Lipocalins Fluorescein 
19603796  
10.1021/bi900535j  
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