Atomic Scale Determination of Enzyme Flexibility and Active Site Stability through Static Modes: Case of Dihydrofolate Reductase-Reference-Cited by-同舟云学术

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Atomic Scale Determination of Enzyme Flexibility and Active Site Stability through Static Modes: Case of Dihydrofolate Reductase

Published:2011-02-02 Issue:7 Volume:115 Page:1616-1622
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Brut Marie¹²³,Estève Alain¹²,Landa Georges¹²,Renvez Guillaume¹²,Djafari Rouhani Mehdi¹²,Vaisset Marc¹²

Affiliation:

1. LAAS-CNRS, Université de Toulouse, 7 avenue du Colonel Roche, F-31077 Toulouse, France

2. Université de Toulouse, UPS, INSA, INP, ISAE, LAAS, F-31077 Toulouse, France

3. Department of Structural Biology, Stanford University School of Medicine, Stanford, California, United States

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp109874z

Reference28 articles.

1. Dihydrofolate reductase as a therapeutic target

2. Protein Dynamics in Enzymatic Catalysis: Exploration of Dihydrofolate Reductase

3. The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

4. Dihydrofolate Reductase: X-ray Structure of the Binary Complex with Methotrexate

5. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.

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