Brunger and his colleagues found that altering the toxin at the binding site by single amino acid changes (obtained from the high resolution crystal structure) drastically reduced its toxicity. (hhmi.org)
They also found that such single amino acid changes occurred at only seven places on its surface — all located near the receptor binding site (the area where the flu virus binds to and infects host cells). (sciencedaily.com)
Using a combination of laboratory assays and computer algorithms, the team tested various mutations in HB36.5, looking for single amino acid changes that would increase how tightly the protein bound to a diverse group of hemagglutinins. (sciencemag.org)