Abstract
Ferlins are complex, multi-domain proteins implicated in diverse functions that range from membrane repair to hearing. The domain structure of ferlin proteins has been assumed to be a fairly simple string of membrane-interacting C2 domains; however, recent advances in in silico protein folding has significantly extended the structural scope of these large proteins. Using AlphaFold2 and RoseTTAfold, we were able to compute unbiased domain boundaries for each of the six human ferlin proteins (dysferlin, myoferlin, otoferlin, Fer1L4,Fer1L5, and Fer1L6).
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