2JDK
Lectin PA-IIL of P.aeruginosa complexed with disaccharide derivative
Summary for 2JDK
| Entry DOI | 10.2210/pdb2jdk/pdb |
| Related | 1GZT 1OUR 1OUS 1OUX 1OVP 1OVS 1OXC 1UZV 1W43 1W8F 1W8H 2BOJ 2BP6 |
| Descriptor | FUCOSE-BINDING LECTIN PA-IIL, alpha-L-fucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose, ... (7 entities in total) |
| Functional Keywords | pseudomonas aeruginosa, lectin, glycomimetic, cystic fibrosis |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 4 |
| Total formula weight | 49527.81 |
| Authors | Marotte, K.,Sabin, C.,Preville, C.,Pymbock, M.,Deguise, I.,Wimmerova, M.,Mitchell, E.P.,Imberty, A.,Roy, R. (deposition date: 2007-01-10, release date: 2007-07-24, Last modification date: 2024-05-08) |
| Primary citation | Marotte, K.,Sabin, C.,Preville, C.,Pymbock, M.,Wimmerova, M.,Mitchell, E.P.,Imberty, A.,Roy, R. X-Ray Structures and Thermodynamics of the Interaction of Pa-Iil from Pseudomonas Aeruginosa with Disaccharide Derivatives. Chemmedchem, 2:1328-, 2007 Cited by PubMed 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. PubMed: 17623286DOI: 10.1002/CMDC.200700100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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