Calibration of Colorimetric Protein Assays for Quantitation of Plant AB Toxins
2000; Elsevier BV; Volume: 284; Issue: 2 Linguagem: Inglês
10.1006/abio.2000.4721
ISSN1096-0309
AutoresMarta Jiménez, Sabine André, Hans‐Joachim Gabius, Dolores Solı́s,
Tópico(s)Plant Parasitism and Resistance
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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