3DCQ
LECB (PA-LII) in complex with the synthetic ligand 2G0
Summary for 3DCQ
| Entry DOI | 10.2210/pdb3dcq/pdb |
| Related | 1OUX 1OXC |
| Descriptor | Fucose-binding lectin PA-IIL, CALCIUM ION, (2S)-1-[(2S)-6-amino-2-({[(2S,3S,4R,5S,6S)-3,4,5-trihydroxy-6-methyltetrahydro-2H-pyran-2-yl]acetyl}amino)hexanoyl]-N-[(1S)-1-carbamoyl-3-methylbutyl]pyrrolidine-2-carboxamide, ... (4 entities in total) |
| Functional Keywords | lectin, carbohydrate, sugar binding protein |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 4 |
| Total formula weight | 49434.06 |
| Authors | Johansson, E.M.,Crusz, S.A.,Kolomiets, E.,Buts, L.,Kadam, R.U.,Cacciarini, M.,Bartels, K.M.,Diggle, S.P.,Camara, M.,Williams, P.,Loris, R.,Nativi, C.,Rosenau, F.,Jaeger, K.E.,Darbre, T.,Reymond, J.L. (deposition date: 2008-06-04, release date: 2009-01-13, Last modification date: 2023-11-01) |
| Primary citation | Johansson, E.M.,Crusz, S.A.,Kolomiets, E.,Buts, L.,Kadam, R.U.,Cacciarini, M.,Bartels, K.M.,Diggle, S.P.,Camara, M.,Williams, P.,Loris, R.,Nativi, C.,Rosenau, F.,Jaeger, K.E.,Darbre, T.,Reymond, J.L. Inhibition and dispersion of Pseudomonas aeruginosa biofilms by glycopeptide dendrimers targeting the fucose-specific lectin LecB. Chem.Biol., 15:1249-1257, 2008 Cited by PubMed Abstract: The human pathogenic bacterium Pseudomonas aeruginosa produces a fucose-specific lectin, LecB, implicated in tissue attachment and the formation of biofilms. To investigate if LecB inhibition disrupts these processes, high-affinity ligands were obtained by screening two 15,536-member combinatorial libraries of multivalent fucosyl-peptide dendrimers. The most potent LecB-ligands identified were dendrimers FD2 (C-Fuc-LysProLeu)(4)(LysPheLysIle)(2)LysHisIleNH(2) (IC(50) = 0.14 microM by ELLA) and PA8 (OFuc-LysAlaAsp)(4)(LysSerGlyAla)(2)LysHisIleNH(2) (IC(50) = 0.11 microM by ELLA). Dendrimer FD2 led to complete inhibition of P. aeruginosa biofilm formation (IC(50) approximately 10 microM) and induced complete dispersion of established biofilms in the wild-type strain and in several clinical P. aeruginosa isolates. These experiments suggest that LecB inhibition by high-affinity multivalent ligands could represent a therapeutic approach against P. aeruginosa infections by inhibition of biofilm formation and dispersion of established biofilms. PubMed: 19101469DOI: 10.1016/j.chembiol.2008.10.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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