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CH-π "T-shape" interaction with histidine explains binding of aromatic galactosides to Pseudomonas aeruginosa lectin LecA.
ACS Chem. Biol. 8, 1925-1930 (2013)
The galactose specific lectin LecA mediates biofilm formation in the opportunistic pathogen P. aeruginosa . The interaction between LecA and aromatic β-galactoside biofilm inhibitors involves an intermolecular CH-π T-shape interaction between C(ε1)-H of residue His50 in LecA and the aromatic ring of the galactoside aglycone. The generality of this interaction was tested in a diverse family of β-galactosides. LecA binding to aromatic β-galactosides (KD ∼ 8 μM) was consistently stronger than to aliphatic β-galactosides (KD ∼ 36 μM). The CH-π interaction was observed in the X-ray crystal structures of six different LecA complexes, with shorter than the van der Waals distances indicating productive binding. Related XH/cation/π-π interactions involving other residues were identified in complexes of aromatic glycosides with a variety of carbohydrate binding proteins such as concanavalin A. Exploiting such interactions might be generally useful in drug design against these targets.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Ch/pi Hydrogen-bond; Center-dot-pi; Crystal-structure; Concanavalin-a; Pa-i; Inhibitors; Design; Conformation; Specificity; Agglutinin
ISSN (print) / ISBN 1554-8929
Journal ACS Chemical Biology
Quellenangaben Volume: 8, Issue: 9, Pages: 1925-1930
Publisher American Chemical Society (ACS)
Publishing Place Washington
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)