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Publication Abstract from PubMed

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(epsilon1)-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 (KD approximately 8 muM) was consistently stronger than to aliphatic beta-galactosides (KD approximately 36 muM). 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.

CH-pi "T-Shape" Interaction with Histidine Explains Binding of Aromatic Galactosides to Pseudomonas aeruginosa Lectin LecA.,Kadam RU, Garg D, Schwartz J, Visini R, Sattler M, Stocker A, Darbre T, Reymond JL ACS Chem Biol. 2013 Sep 20;8(9):1925-30. doi: 10.1021/cb400303w. Epub 2013 Jul, 31. PMID:23869965^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.