Title : Changes in the electron density of the cofactor NADPH on binding to E. coli dihydrofolate reductase.

Pub. Date : 1991

PMID : 1758881






2 Functional Relationships(s)
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1 Further calculations on proposed enzyme mutants show that the polarization of NADPH on binding to DHFR is, in large part, induced by a motif of three positively charged residues. NADP dihydrofolate reductase Escherichia coli
2 The possibility of this long-range polarization of NADPH was originally proposed based on a previous study of ligand binding to DHFR where a conserved structural motif of three positively charged residues was found to play a major role in polarizing the substrate folate over its entire length of 18 A. NADP dihydrofolate reductase Escherichia coli