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Molecular dissection of dystrophin identifies the docking site for nNOS

At current count, we human beings have 20,687 protein-coding genes encoded within our DNA (1). The unfortunate reality is that we know very little about the functions of most of these proteins. Because new scientific discovery is built upon the foundation of prior work, it is perhaps obvious that knowledge gaps like these can have compounding effects to slow further scientific advancement. Indeed, imagine the state of molecular biology and biotechnology today if Watson and Crick’s publication of DNA structure had been reported just a few decades earlier. So too is the case for translational research: it is difficult to develop treatments for a genetic disorder when we do not understand the affliction’s pathogenic mechanisms. Thus, the more basic knowledge we possess about the function of a given disease gene and its protein product, the more ammunition we have to design rational therapies. In PNAS, Lai et al. from the Duan laboratory at the University of Missouri provide an exquisite example of a basic study on protein structure and function with potentially important translational implications for therapy of Duchenne muscular dystrophy (DMD) (2).