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Article

Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase.

Biochemistry - 12 Jan 2016

Duff Michael R, Chopra Shaileja, Strader Michael Brad, Agarwal Pratul K, Howell Elizabeth E

Abstract excerpt

Homotetrameric R67 dihydrofolate reductase possesses 222 symmetry and a single active site pore. This situation results in a promiscuous binding site that accommodates either the substrate, dihydrofolate (DHF), or the cofactor, NADPH. NADPH interacts more directly with the protein as it is larger than the substrate. In contrast, the p-aminobenzoyl-glutamate tail of DHF, as monitored by nuclear magnetic resonance...

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Source

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Identifiers

PMID: 26637016
DOI: 10.1021/acs.biochem.5b00981
PMCID: PMC5147970

Genes

DHFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase.PMID 26637016Read ↗

Defining the binding site of homotetrameric R67 dihydrofolate reductase and correlating binding enthalpy with catalysis.Semantic proximity Read ↗

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"Catch 222," the effects of symmetry on ligand binding and catalysis in R67 dihydrofolate reductase as determined by mutations at Tyr-69.Semantic proximity Read ↗

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