Solving the structures of mammalian BESTROPHINs and TMEM16s
The mammalian 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).
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Elucidating the pathological mechanisms of CaCC-related diseases
BESTROPHINs and TMEM16s are directly connected to human diseases. For instance, mutations of BESTROPHIN1 (BEST1) cause vision threatening retinal degenerations, while up-regulated TMEM16A activity has been clinically linked to asthma, hypertension and numerous cancers. Therefore, it is of great biomedical and pharmaceutical value to understand how these events translate into physiological abnormalities and ultimately become pathogenic.
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