arrow3 Comments
  1. Ash
    Mar 26 - 12:01 pm

    Great study and post! As always, nature is cleverer than we imagine it to be. Is it harder for the enzyme to mutate “inside” residues than “outside” ones? Because if that’s the case then a better strategy might be to just get rid of the outside-binding functionality and focus on getting affinity through inside-binding alone.

  2. See Arr Oh
    Mar 26 - 12:10 pm

    Ash – Good catch. The authors don’t specify whether one mutation or another is “harder,” per se, but they do indicate that the three common mutations they observe occur at Phe(33), Thr(67), and Pro(69), all of which are “outer” residues. Seems to me they could capitalize on that grey-colored pocket either with larger anilines, or a replacement for the pterin section altogether.

  3. gippgig
    Apr 02 - 2:27 am

    It is harder to mutate “inside” residues because changing an internal residue is more likely to alter the 3-D structure (which often inactivates the enzyme).

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