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|4foq, resolution 1.99Å ()|
|Gene:||nanB, SP_1687 (Streptococcus pneumoniae)|
|Related:||2vw0, 2vw1, 2vw2, 4fov, 4fow, 4foy, 4fp2, 4fp3, 4fpc, 4fpe, 4fpf, 4fpg, 4fph, 4fpj, 4fpk, 4fpl, 4fpo, 4fpy, 4fq4|
Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-aminoethanesulfonic acid
The major human pathogen Streptococcus pneumoniae plays a key role in several disease states including septicaemia, meningitis and community-acquired pneumonia. Although vaccines against S. pneumoniae are available as prophylactics, there remains a need to identify and characterise novel chemical entities that can treat the diseases caused by this pathogen. S. pneumoniae expresses three sialidases, enzymes that cleave sialic acid from carbohydrate-based surface molecules. Two of these enzymes, NanA and NanB, have been implicated in the pathogenesis of S. pneumoniae and are considered to be validated drug targets. Here we report our studies on the synthesis and structural characterisation of novel NanB-selective inhibitors that are inspired by the beta-amino-sulfonic acid family of buffers.
Synthesis and structural characterisation of selective non-carbohydrate-based inhibitors of bacterial sialidases., Brear P, Telford J, Taylor GL, Westwood NJ, Chembiochem. 2012 Nov 5;13(16):2374-83. doi: 10.1002/cbic.201200433. Epub 2012, Oct 15. PMID:23070966
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.