Journal
ACS CHEMICAL BIOLOGY
Volume 8, Issue 9, Pages 1925-1930Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb400303w
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- University of Berne
- Swiss National Science Foundation
- COST Action [D34]
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The galactose specific lectin LecA mediates biofilm formation in the opportunistic pathogen P. aeruginosa. The interaction between LecA and aromatic beta-galactoside biofilm inhibitors involves an intermolecular CH-pi T-shape interaction between C(epsilon 1)-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 beta-galactosides. LecA binding to aromatic beta-galactosides (K-D similar to 8 mu M) was consistently stronger than to aliphatic beta-galactosides (K-D similar to 36 mu M). The CH-pi 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/pi-pi 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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