View publication

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

(click to unfold)
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 
10 (Last update: 03/16/2019 6:45:37pm)