Engineering a rhodopsin protein mimic.

Rachael M Crist; Chrysoula Vasileiou; Montserrat Rabago-Smith; James H Geiger; Babak Borhan

doi:10.1021/ja058591m

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Engineering a rhodopsin protein mimic.

Rachael M Crist·Chrysoula Vasileiou·Montserrat Rabago-Smith·James H Geiger·Babak Borhan

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Abstract

Due to the difficulties in handling and manipulating membrane-bound proteins, such as rhodopsin, and the lack of crystallographic information on the cone opsins, we have opted to engineer a protein mimic of the transmembrane G-protein coupled receptor. Human cellular retinoic acid binding protein (CRABPII), a well studied and characterized protein, has been reengineered into a protein that now will bind retinal as a protonated Schiff base with high binding affinity (Kd = 2 nM) mimicking that of rhodopsin.

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Binding Sites Biomimetic Materials Crystallography, X-Ray Humans Kinetics Lysine Protein Engineering Receptors, Retinoic Acid Rhodopsin Spectrometry, Fluorescence Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spectrophotometry, Ultraviolet Thermodynamics Tretinoin Journal Article Research Support, N.I.H., Extramural

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Rachael M Crist, Chrysoula Vasileiou, Montserrat Rabago-Smith, James H Geiger, Babak Borhan. 2006-04-12. Engineering a rhodopsin protein mimic.. https://doi.org/10.1021/ja058591m

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