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

2023-08-02

Abstract excerpt

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. We determined cryo-electron microscopy structures of human MTHFR bound to SAM and its demethylated product S-adenosyl-L-homocy...

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Literature Corpus work
e4dbd03f-1b34-5bff-8c32-c60c79676313
DOI
10.1101/2023.08.02.551630
Open publication

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Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductaseDOI 10.1101/2023.08.02.551630
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