One tiny microscopic tweak can completely flip what a protein is attracted to, even if the protein's shape doesn't change at all.
April 10, 2026
Original Paper
Altered carbohydrate preference in structurally conserved PLL lectin family revealed by newly characterized PHL2
SSRN · 6550910
The Takeaway
Researchers found that a specific protein family can change its entire function—switching from binding one type of sugar to another—with only a minor structural change. This shows that the biological 'keys' of life are far more sensitive and adaptable than their general appearance suggests.
From the abstract
The PLL lectin family (PLLs) comprises structurally conserved lectins originating from a pathogenic bacteria of the genus Photorhabdus. Here, we characterize PHL2, a newly identified member of this family encoded in Photorhabdus asymbiotica, a potent insect pathogen and an emerging human pathogen associated with difficult-to-treat wound infections. We investigated the carbohydrate-binding properties of recombinant PHL2 using glycan array screening and isothermal titration calorimetry, and analys