Literature summary for 1.5.1.3 extracted from

Cody, V.; Pace, J.; Rosowsky, A.
Structural analysis of a holoenzyme complex of mouse dihydrofolate reductase with NADPH and a ternary complex with the potent and selective inhibitor 2,4-diamino-6-(2-hydroxydibenz[b,f]azepin-5-yl)methylpteridine (2008), Acta Crystallogr. Sect. D, 64, 977-984.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
holo and ternary complexes with NADPH and the inhibitor 2,4-diamino-6-(2-hydroxydibenz[b,f]azepin-5-yl)methylpteridine, to 1.9 and 1.4 A resolution, respectively. Modeling data of inhibitor 4-([5-[(2,4-diaminopteridin-6-yl)methyl]-5H-dibenzo[b,f]azepin-2-yl]oxy)butane-1,1-diol in the active site indicate that binding would require ligand-induced conformational changes to the enzyme for the inhibitor to fit or that the inhibitor side-chain would have to adopt an alternative binding mode to that observed for similar inhibitors. The complexes have a decreased active-site volume compared with complexes of the enzyme from Pneumocystis carinii	Mus musculus
modeling data of inhibitor PT682 in the active site indicate that binding would require ligand-induced conformational changes to the enzyme for the inhibitor to fit or that the inhibitor side-chain would have to adopt an alternative binding mode to that observed for similar inhibitors. The complexes have an increased active-site volume compared with complexes of the enzyme from Mus musculus	Pneumocystis carinii

Crystallization (Comment)

Organism

holo and ternary complexes with NADPH and the inhibitor 2,4-diamino-6-(2-hydroxydibenz[b,f]azepin-5-yl)methylpteridine, to 1.9 and 1.4 A resolution, respectively. Modeling data of inhibitor 4-([5-[(2,4-diaminopteridin-6-yl)methyl]-5H-dibenzo[b,f]azepin-2-yl]oxy)butane-1,1-diol in the active site indicate that binding would require ligand-induced conformational changes to the enzyme for the inhibitor to fit or that the inhibitor side-chain would have to adopt an alternative binding mode to that observed for similar inhibitors. The complexes have a decreased active-site volume compared with complexes of the enzyme from Pneumocystis carinii

Mus musculus

modeling data of inhibitor PT682 in the active site indicate that binding would require ligand-induced conformational changes to the enzyme for the inhibitor to fit or that the inhibitor side-chain would have to adopt an alternative binding mode to that observed for similar inhibitors. The complexes have an increased active-site volume compared with complexes of the enzyme from Mus musculus

Pneumocystis carinii

Inhibitors

Inhibitors	Comment	Organism
2,4-diamino-6-(2-hydroxydibenz[b,f]azepin-5-yl)methylpteridine	crystallization data	Mus musculus
4-([5-[(2,4-diaminopteridin-6-yl)methyl]-5H-dibenzo[b,f]azepin-2-yl]oxy)butane-1,1-diol	O-(3-carboxypropyl) inhibitor, crystallization data	Mus musculus
PT682	O-(3-carboxypropyl) inhibitor, crystallization data	Pneumocystis carinii

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P00375	-	-
Pneumocystis carinii	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Mus musculus