Solving the structures of mammalian BESTROPHINs and TMEM16s
BESTROPHIN and TMEM16 families consist of four and ten members, respectively. Solving their three-dimensional protein structures will not only provide molecular bases of their functional properties including conductivity, selectivity and gating, but also reveal instructive clues for pharmaceutical development (Yang et al. Science 2014). We aim to encounter this task by state of the art cryo-EM and X-ray crystallography. Once the protein structure is obtained, patient-specific mutations can be introduced to analyze the associated structural alterations, which are essential for understanding the disease-causing mechanisms of the mutations.
« back to all projects