Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductase

Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductase

Abstract 5,10-methylenetetrahydrofolate reductase (MTHFR) commits folate-derived one-carbon units to generate the methyl-donor s-adenosyl-l-methionine (SAM). Eukaryotic MTHFR appends to the well-conserved catalytic domain (CD) a unique regulatory domain (RD) that confers feedback inhibition by SAM....

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Bibliographic Details
Main Authors: Linnea K. M. Blomgren, Melanie Huber, Sabrina R. Mackinnon, Céline Bürer, Arnaud Baslé, Wyatt W. Yue, D. Sean Froese, Thomas J. McCorvie
Format: Article
Language:English
Published: Nature Portfolio 2024-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-024-47174-y

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https://doi.org/10.1038/s41467-024-47174-y

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