CH−π “T-Shape” Interaction
with Histidine Explains Binding of Aromatic Galactosides to Pseudomonas aeruginosa Lectin LecA
Rameshwar
U. Kadam
Divita Garg
Julian Schwartz
Ricardo Visini
Michael Sattler
Achim Stocker
Tamis Darbre
Jean-Louis Reymond
10.1021/cb400303w.s001
https://acs.figshare.com/articles/journal_contribution/CH__T_Shape_Interaction_with_Histidine_Explains_Binding_of_Aromatic_Galactosides_to_Pseudomonas_aeruginosa_Lectin_LecA/2025810
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 (<i>K</i><sub>D</sub> ∼
8 μM) was consistently stronger than to aliphatic β-galactosides
(<i>K</i><sub>D</sub> ∼ 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.
2015-12-16 23:35:04
lectin LecA mediates biofilm formation
XH
carbohydrate binding proteins
Aromatic Galactosides
CH
LecA complexes
LecA binding
galactoside aglycone
Pseudomonas aeruginosa Lectin LecAThe galactose
pathogen P
van der Waals distances
interaction
KD
drug design