Journal
FEBS LETTERS
Volume 582, Issue 15, Pages 2309-2312Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.05.035
Keywords
agglutinin; lectin; mistletoe; ribosome-inactivating protein; ricin
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Mistletoe lectin is a potent biohazard. Lectin activity in the toxic dimer primarily originates from the 2 gamma-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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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