De novo "Gator" ligand binding protein published in Nature Chemistry

DGL post-doc Nick Polizzi's work on a de novo synthetic porphyrin binding protein will be included in the August 21 edition of Nature Chemistry, and is now published in advance online. The protein, nicknamed "Gator" for it's jaw-like motion observed upon porphyrin binding, is the first ligand-binding protein designed from scratch whose structure has been determined experimentally, and it matches the design with sub-angstrom accuracy!

Enzymes in nature bind and utilize cofactors like porphyrin, and this work elucidated a core design principle integral to successful binding and positioning of the cofactor in the de novo gator protein. This effort puts researchers one step closer to being able to build custom functional enzymes from scratch!

*Polizzi NF, *Wu Y, *Lemmin T, *Maxwell AM, *Zhang SQ, Rawson J, Beratan DN, Therien MJ, DeGrado WF. De novo design of a hyperstable non-natural protein–ligand complex with sub-Å accuracy. Nature Chemistry. 2017.

*DGL members

This project was a close collaboration with the groups of Dr. Beratan and Dr. Therien at Duke University.