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1w0o
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0o RCSB], [http://www.ebi.ac.uk/pdbsum/1w0o PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0o RCSB], [http://www.ebi.ac.uk/pdbsum/1w0o PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NANH_VIBCH NANH_VIBCH]] Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections. Facilitates cholera toxin binding to host intestinal epithelial cells by converting cell surface polysialogangliosides to GM1 monogangliosides. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 14:05, 25 December 2014
VIBRIO CHOLERAE SIALIDASE
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