ABCG5/G8 Crystallization in a Lipidic Bicelle Environment for X-Ray Crystallography

Hello, my team study type of protein loss span across the cellular membrane, and we are looking at the relationship to the medicine and biology. Specifically, we are looking at one particular protein which would require ATP to drive its function, and then it, the name is called ATP binding cassette transporter. In particular, we are looking at their fundamental structure function relationship, and then use that to understand a lot of chronic disease, especially cardiovascular disease.

Due to the complexity of purifying the membrane proteins and their stability at native temperatures, obtaining 3D protein crystals is the main challenge in the field, and it also limits the drug discovery applications. Our team has established methods in cryo-EM and X-Ray crystallography for the structural studies of membrane transporter proteins. And previously our lab also solved the crystal structure of the first human ABCG5/G8 obligate heterodimer, in both apo as well as cholesterol-bound states.

Our results can provide a breakthrough in small molecule drug discovery or drug repurposing. Obtaining 3D protein crystals can also enable soaking experiments for the cocrystallization of protein and ligand complexes. Our laboratory aims to determine the molecular basis of lipid recognition and translocation by ATP dependent lipid transporter proteins.

And we also aim to establish new methods in drug development for studying the molecular dynamics and structural aspects of ABC transporters.