4cpb

CRYSTAL STRUCTURE OF LECA IN COMPLEX WITH A DIVALENT GALACTOSIDE AT 1. 57 ANGSTROM IN MAGNESIUM

spinqualitylabelsall models 4cpb, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cpb is a 4 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.57Å Ligands: 2PE, CA, CL, CN8, EDO, GAL, OCS, PEG, TRO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PA1L_PSEAE D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl-beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity. Publication Abstract from PubMed Lectin LecA is a virulence factor of Pseudomonas aeruginosa involved in lung injury, mortality, and cellular invasion. Ligands competing with human glycoconjugates for LecA binding are thus promising candidates to counteract P. aeruginosa infections. We have identified a novel divalent ligand from a focused galactoside(Gal)-conjugate array which binds to LecA with very high affinity (Kd = 82 nM). Crystal structures of LecA complexed with the ligand together with modeling studies confirmed its ability to chelate two binding sites of LecA. The ligand lowers cellular invasiveness of P. aeruginosa up to 90 % when applied in the range of 0.05-5 muM. Hence, this ligand might lead to the development of drugs against P. aeruginosa infection. A LecA ligand identified from a galactoside-conjugate array inhibits host cell invasion by Pseudomonas aeruginosa.,Novoa A, Eierhoff T, Topin J, Varrot A, Barluenga S, Imberty A, Romer W, Winssinger N Angew Chem Int Ed Engl. 2014 Aug 18;53(34):8885-9. doi: 10.1002/anie.201402831., Epub 2014 Jul 7. PMID:25044671 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactose-binding lectin

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