2JDH: Lectin Pa-iil Of P.aeruginosa Complexed With Disaccharide Derivative

Citation:
Abstract
Pseudomonas aeruginosa is an opportunistic bacterium showing increasing resistance to antibiotics and consequently represents elevated threatening problems in hospital environments, particularly for cystic fibrosis patients. The use of glycomimetics as an anti-adhesive strategy against microorganisms may complement the use of antibiotics. PA-IIL lectin (LecB) from P. aeruginosa constitutes an appealing target for antibacterial agents, as it has been proposed to play a key role in binding to airway epithelia and/or to be involved in biofilm formation. The lectin has an unusually high affinity for L-fucose and related oligosaccharides. In the work presented herein, the disaccharide alphaFuc1-4GlcNAc is used as a scaffold toward the synthesis of a series of glycomimetic derivatives. Microcalorimetry and structural studies indicate that several of the derivatives are potent inhibitors of the lectin, with affinity in the same range as the best known natural ligand, Lewis a, and could represent interesting leads for the development of future antibacterial compounds.
PDB ID: 2JDHDownload
MMDB ID: 53749
PDB Deposition Date: 2007/1/9
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 1.1  Å
Source Organism:
Similar Structures:
Biological Unit for 2JDH: tetrameric; determined by software (PQS)
Molecular Components in 2JDH
Label Count Molecule
Proteins (4 molecules)
4
Fucose-binding Lectin Pa-iil
Molecule annotation
Chemicals (19 molecules)
1
4
2
8
3
3
4
3
5
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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