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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
Author(s) -
Jiménez Marta,
André Sabine,
Barillari Caterina,
Romero Antonio,
Rognan Didier,
Gabius Hans-Joachim,
Solís Dolores
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.05.035
Subject(s) - lectin , ricin , viscum album , chemistry , ribosome inactivating protein , dimer , ligand (biochemistry) , protein subunit , c type lectin , mannan binding lectin , cd69 , biochemistry , binding site , biophysics , stereochemistry , biology , receptor , in vitro , organic chemistry , ribosome , ecology , rna , gene , toxin , cytotoxic t cell , il 2 receptor
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.