4fp3: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-[(Furan-2-ylmethyl)ammonio]sulfonate== | ==Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-[(Furan-2-ylmethyl)ammonio]sulfonate== | ||
<StructureSection load='4fp3' size='340' side='right' caption='[[4fp3]], [[Resolution|resolution]] 2.74Å' scene=''> | <StructureSection load='4fp3' size='340' side='right'caption='[[4fp3]], [[Resolution|resolution]] 2.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fp3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4fp3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FP3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IJ2:2-[(FURAN-2-YLMETHYL)AMINO]ETHANESULFONIC+ACID'>IJ2</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IJ2:2-[(FURAN-2-YLMETHYL)AMINO]ETHANESULFONIC+ACID'>IJ2</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fp3 OCA], [https://pdbe.org/4fp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fp3 RCSB], [https://www.ebi.ac.uk/pdbsum/4fp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fp3 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/NANB_STRPN NANB_STRPN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 21: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Neuraminidase|Neuraminidase]] | *[[Neuraminidase 3D structures|Neuraminidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus pneumoniae]] | ||
[[Category: | [[Category: Brear P]] | ||
Latest revision as of 23:04, 19 October 2022
Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-[(Furan-2-ylmethyl)ammonio]sulfonateCrystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-[(Furan-2-ylmethyl)ammonio]sulfonate
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|