ArticleBiophysical journal2010
Tryptophan as a molecular shovel in the glycosyl transfer activity of Trypanosoma cruzi trans-sialidase.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- Analysis of Glycan Recognition by Concanavalin A Using Absolute Binding Free Energy Calculations.Journal of chemical information and modeling · 2024Article
- Molecular Dynamics Simulations Reveal the Conformational Transition of GH33 Sialidases.International journal of molecular sciences · 2023Article
- Synthesis of Human Milk Oligosaccharides: Protein Engineering Strategies for Improved Enzymatic Transglycosylation.Molecules (Basel, Switzerland) · 2019Review
- It All Starts with a Sandwich: Identification of Sialidases with Trans-Glycosylation Activity.PloS one · 2016Article
- Evidence of ternary complex formation in Trypanosoma cruzi trans-sialidase catalysis.The Journal of biological chemistry · 2014Article
- Conformational dynamics of dry lamellar crystals of sugar based lipids: an atomistic simulation study.PloS one · 2014Article
- Insights into the activity and specificity of Trypanosoma cruzi trans-sialidase from molecular dynamics simulations.Biochemistry · 2013Article
- Sialic acid: a sweet swing between mammalian host and Trypanosoma cruzi.Frontiers in immunology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular dynamics investigations into active site plasticity of Trypanosoma cruzi trans-sialidase, a protein implicated in Chagas disease, suggest that movement of the Trp(312) loop plays an important role in the enzyme's sialic acid transfer mechanism. The observed Trp(312) flexibility equates to a molecular shovel action, which leads to the expulsion of the donor aglycone leaving group from the catalytic site. These computational simulations provide detailed structural insights into sialyl transfer by the trans-sialidase and may aid the design of inhibitors effective against this neglected tropical disease.
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