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Sialidase

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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='2w68' size='340' side='right' caption='Caption for this structure' scene=''>
== Function ==
== Function ==
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'''Sialidase''' is a neuraminidase which cleaves terminal sialic acid from a variety of natural substances <ref>PMID:12374200</ref>. For '''Trans-sialidase''' see [[Neuraminidase]]. '''Anhydrosialidase''' catalyzes the elimination of sialyl group in N-acetylneuraminic acid glycosides to yield 2,7-anhydro-α-N-acetylneuraminate.
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'''Sialidase''' is a neuraminidase which cleaves terminal sialic acid from a variety of natural substances <ref>PMID:12374200</ref>. The sialic acid-binding domain of sialidase is called CBD. For '''Anhydrosialidase''' catalyzes the elimination of sialyl group in N-acetylneuraminic acid glycosides to yield 2,7-anhydro-α-N-acetylneuraminate. For '''Trans-sialidase''' see [[Neuraminidase]].
== Disease ==
== Disease ==
== Relevance ==
== Relevance ==
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''Trypanosoma cruzi'' trans-sialidase is a drug target agains Chagas Disease<ref>PMID:24144418</ref>.
 
== Structural highlights ==
== Structural highlights ==
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**[[1n1v]] – TrSal + neuraminic acid derivative <br />
**[[1n1v]] – TrSal + neuraminic acid derivative <br />
**[[1mz6]], [[1n1t]], [[2ags]] – TrSal + inhibitor <br />
**[[1mz6]], [[1n1t]], [[2ags]] – TrSal + inhibitor <br />
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**[[1n1y]]– TrSal + sialic acid <br />
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**[[1n1y]] – TrSal + sialic acid <br />
**[[2a75]], [[2fhr]] – TrSal + sialic acid derivative<br />
**[[2a75]], [[2fhr]] – TrSal + sialic acid derivative<br />
**[[1dim]], [[1dil]], [[2sil]], [[2sim]] – StSal + inhibitor <br />
**[[1dim]], [[1dil]], [[2sil]], [[2sim]] – StSal + inhibitor <br />

Revision as of 08:41, 7 November 2018

Caption for this structure

Drag the structure with the mouse to rotate

3D structures of salidase

Updated on 07-November-2018

References

  1. Monti E, Preti A, Venerando B, Borsani G. Recent development in mammalian sialidase molecular biology. Neurochem Res. 2002 Aug;27(7-8):649-63. PMID:12374200

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Michal Harel, Alexander Berchansky, Jaime Prilusky

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