Domain versatility in plant AB‐toxins: Evidence for a local, pH‐dependent rearrangement in the 2γ lectin site of the mistletoe lectin by applying ligand derivatives and modelling
2008; Wiley; Volume: 582; Issue: 15 Linguagem: Inglês
10.1016/j.febslet.2008.05.035
ISSN1873-3468
AutoresMarta Jiménez, Sabine André, Caterina Barillari, Antonio Romero, Didier Rognan, Hans‐Joachim Gabius, Dolores Solı́s,
Tópico(s)Transgenic Plants and Applications
ResumoMistletoe lectin is a potent biohazard. Lectin activity in the toxic dimer primarily originates from the 2γ‐subdomain (Tyr‐site) of the B‐subunit. Crystallographic information on lectin–sugar complexes is available only at acidic pH, where lectin activity is low. Thus, we mapped ligand‐binding properties including comparison to ricin's Tyr‐site at neutral pH. Using these results and molecular dynamics simulations, a local conformational change was rendered likely. The obtained structural information is valuable for the design of potent inhibitors.
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