NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions-Reference-Cited by-同舟云学术

NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions

Published:2011-04-14 Issue:18 Volume:50 Page:3609-3620
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Feeney James¹,Birdsall Berry¹,Kovalevskaya Nadezhda V.²,Smurnyy Yegor. D.²,Navarro Peran Emna M.¹,Polshakov Vladimir I.¹³

Affiliation:

1. Division of Molecular Structure, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, U.K.

2. Chemistry Department, M.V.Lomonosov Moscow State University, Moscow 119991, Russia

3. Center for Magnetic Tomography & Spectroscopy, Faculty of Fundamental Medicine, M.V.Lomonosov Moscow State University, Moscow 119991, Russia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200067t

Reference65 articles.

1. Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim.

2. A kinetic study of wild-type and mutant dihydrofolate reductases from Lactobacillus casei

3. Structure and energetics of ligand binding to proteins:Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system

4. Binding of coenzyme analogs to Lactobacillus casei dihydrofolate reductase: binary and ternary complexes

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