Microsecond timescale MD simulations at the transition state of PmHMGR predict remote allosteric residues-Reference-Cited by-同舟云学术

Microsecond timescale MD simulations at the transition state of PmHMGR predict remote allosteric residues

Published:2021 Issue:18 Volume:12 Page:6413-6418
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Quinn Taylor R.¹²³⁴⁵^ORCID,Steussy Calvin N.⁶⁷⁸⁹⁴^ORCID,Haines Brandon E.¹⁰¹¹¹²⁴^ORCID,Lei Jinping¹⁰¹³¹⁴¹⁵¹⁶,Wang Wei¹⁰¹³¹⁴¹⁵,Sheong Fu Kit¹⁰¹³¹⁴¹⁵,Stauffacher Cynthia V.⁶⁷⁸⁹⁴^ORCID,Huang Xuhui¹⁰¹³¹⁴¹⁵^ORCID,Norrby Per-Ola¹²³⁴¹⁷^ORCID,Helquist Paul¹²³⁴^ORCID,Wiest Olaf¹²³⁴¹⁸^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry

2. University of Notre Dame

3. Notre Dame

4. USA

5. Early TDE Discovery, Early Oncology

6. Department of Biological Sciences

7. Purdue Center for Cancer Research

8. Purdue University

9. West Lafayette

10. Department of Chemistry

11. Westmont College

12. Santa Barbara

13. The Hong Kong University of Science and Technology

14. Kowloon

15. China

16. School of Pharmaceutical Sciences

17. Data Science and Modelling

18. Lab of Computational Chemistry and Drug Design

Abstract

Transition state force fields enable MD simulations at the transition state of HMGCoA reductase that sample the transition state ensemble on the μs timescale to identify remote residues that affect the reaction rate.

Funder

National Institute of General Medical Sciences

Research Grants Council, University Grants Committee

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/SC/D1SC00102G

Reference29 articles.

1. Molecular Architecture and Biological Reactions

2. Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase