Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+complex reveals a novel cofactor binding mode
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Reference18 articles.
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3. Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein;Bradrick;Biochemistry,1996
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1. Pharmacophore Binding Motifs for Nicotinamide Adenine Dinucleotide Analogues Across Multiple Protein Families: A Detailed Contact-Based Analysis of the Interaction between Proteins and NAD(P) Cofactors;Journal of Medicinal Chemistry;2013-07-26
2. Further Studies on the Role of Water in R67 Dihydrofolate Reductase;BIOCHEMISTRY-US;2013
3. Novel crystallization conditions for tandem variant R67 DHFR yield a wild-type crystal structure;Acta Crystallographica Section F Structural Biology and Crystallization Communications;2011-10-25
4. R67, the Other Dihydrofolate Reductase: Rational Design of an Alternate Active Site Configuration;Biochemistry;2007-12-18
5. Crystal Structure of a Type II Dihydrofolate Reductase Catalytic Ternary Complex;Biochemistry;2007-12-01
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