Key residues of the receptor binding domain in the spike protein of SARS-CoV-2 mediating the interactions with ACE2: a molecular dynamics study-Reference-Cited by-同舟云学术

Key residues of the receptor binding domain in the spike protein of SARS-CoV-2 mediating the interactions with ACE2: a molecular dynamics study

Published:2021 Issue:20 Volume:13 Page:9364-9370
ISSN:2040-3364
Container-title:Nanoscale
language:en
Short-container-title:Nanoscale

Author:

Yang Yanmei¹²³⁴⁵^ORCID,Zhang Yunju⁶⁷⁸⁹,Qu Yuanyuan⁶⁷⁸⁹^ORCID,Zhang Chao¹⁰¹¹¹²¹³⁹,Liu Xue-Wei¹⁴¹⁵¹⁶¹⁷¹⁸^ORCID,Zhao Mingwen⁶⁷⁸⁹^ORCID,Mu Yuguang¹⁹¹⁶²⁰¹⁸^ORCID,Li Weifeng⁶⁷⁸⁹^ORCID

Affiliation:

1. College of Chemistry

2. Chemical Engineering and Materials Science

3. Collaborative Innovation Center of Functionalized Probes for Chemical Imaging in Universities of Shandong

4. Key Laboratory of Molecular and Nano Probes

5. Ministry of Education

6. School of Physics

7. Shandong University

8. Jinan

9. China

10. Collaborative Innovation Center of Light Manipulations and Applications

11. School of Physics and Electronics

12. Shandong Normal University

13. Jinan 250358

14. Division of Chemistry and Biological Chemistry

15. School of Physical and Mathematical Sciences

16. Nanyang Technological University

17. Singapore 637371

18. Singapore

19. School of Biological Sciences

20. 637650

Abstract

The residues of RBD in SARS-CoV-2 Spike protein were classified by their contributions to the binding affinity with ACE2. These residues are potential targets to the design of SARS-CoV-2 drugs and identification of cross-active antibodies.

Funder

Natural Science Foundation of Shandong Province

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

Link

http://pubs.rsc.org/en/content/articlepdf/2021/NR/D1NR01672E

Reference39 articles.

1. A pneumonia outbreak associated with a new coronavirus of probable bat origin

2. A new coronavirus associated with human respiratory disease in China