ArticleTrends in biochemical sciences2010
Polymorphisms and disease: hotspots of inactivation in methyltransferases.
Article in Trends in biochemical sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Insights from molecular dynamics simulations for computational protein design.Molecular systems design & engineering · 2017Article
- A Multi-scale Computational Platform to Mechanistically Assess the Effect of Genetic Variation on Drug Responses in Human Erythrocyte Metabolism.PLoS computational biology · 2016Article
- New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities.Structure (London, England : 1993) · 2016Article
- Recognition of methylated DNA through methyl-CpG binding domain proteins.Nucleic acids research · 2012Article
- Structural effects of the L145Q, V157F, and R282W cancer-associated mutations in the p53 DNA-binding core domain.Biochemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Methyltransferases catalyze the methylation processes essential for protein/DNA repair, transcriptional regulation, and drug metabolism in vivo. More than 500 human methyltransferase polymorphisms have been identified, many of which are linked to disease. We mapped all available coding polymorphisms of seven methyltransferases onto their structures to address their structural significance, and identified a polymorphic hotspot ∼20Å from the active site in four of the proteins. Molecular dynamics simulations of these proteins reveal a common mechanism of destabilization: the mutations alter important side-chain contacts within the polymorphic site that are propagated through the protein, thereby distorting the active site. We propose that this hotspot might have arisen to modulate enzymatic activity, with decreased activity actually conferring an advantage in three of the four methyltransferases.
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