Research Article
Investigation on the Binding and Conformational Change of All-trans-Retinoic Acid with Peptidyl Prolyl cis/trans Isomerase Pin1 Using Spectroscopic and Computational Techniques
Figure 6
ATRA binds to Pin1 through key residues. (a) Fluorescence titration of Pin1 and its mutants in the absence and presence of ATRA; λex = 295 nm; T = 293 K; cpin1 or mutants = 5 μM; cATRA = 0, 0.5, 1, 2, 3, 4, and 5 μM. (b) Relative binding constant of ATRA to Pin1 and its mutants. (c) DARTS assay of Pin1 and its mutants by ATRA. (d, e) RMSD of K63A-ATRA and R69A-ATRA complex during 50 ns MD simulation.
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