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PDBsum entry 4ljh
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Sugar binding protein
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PDB id
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4ljh
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References listed in PDB file
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Key reference
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Title
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Ch-π &Quot;t-Shape" interaction with histidine explains binding of aromatic galactosides to pseudomonas aeruginosa lectin leca.
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Authors
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R.U.Kadam,
D.Garg,
J.Schwartz,
R.Visini,
M.Sattler,
A.Stocker,
T.Darbre,
J.L.Reymond.
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Ref.
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Acs Chem Biol, 2013,
8,
1925-1930.
[DOI no: ]
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PubMed id
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Abstract
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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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