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
Jan 1, 2008·
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Jiménez, M.
André, S.
Barillari, C.
Romero, A.
Rognan, D.
Gabius, H.
Solís, D.
Abstract
Mistletoe 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.
Type
Publication
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, FEBS Letters 2008 582 (15), 2309-2312