Targeting trimeric transmembrane domain 5 of oncogenic latent membrane protein 1 using a computationally designed peptide-Reference-Cited by-同舟云学术

Targeting trimeric transmembrane domain 5 of oncogenic latent membrane protein 1 using a computationally designed peptide

Published:2019 Issue:32 Volume:10 Page:7584-7590
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Wang Yibo¹²³⁴⁵,Peng Yinghua⁶⁷⁸⁴⁵,Zhang Bo¹²³⁴⁵,Zhang Xiaozheng¹²³⁴⁵,Li Hongyuan¹²³⁴⁵,Wilson Andrew J.⁹¹⁰¹¹¹²¹³^ORCID,Mineev Konstantin S.¹⁴¹⁵¹⁶¹⁷,Wang Xiaohui¹²³⁴⁵^ORCID

Affiliation:

1. Laboratory of Chemical Biology

2. Changchun Institute of Applied Chemistry

3. Chinese Academy of Sciences

4. Changchun

5. China

6. State Key Laboratory for Molecular Biology of Special Wild Economic Animals

7. Institute of Special Animal and Plant Sciences

8. Chinese Academy of Agricultural Sciences

9. School of Chemistry

10. University of Leeds

11. Leeds

12. UK

13. Astbury Centre for Structural Molecular Biology

14. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

15. Russian Academy of Sciences

16. Moscow

17. Russian

Abstract

A peptide inhibitor was designed in silico and validated experimentally to disrupt homotrimeric transmembrane helix assembly.

Funder

Natural Science Foundation of Jilin Province

National Natural Science Foundation of China

Chinese Academy of Sciences

Chinese Academy of Agricultural Sciences

State Key Laboratory of Oncology in South China

Central Public-interest Scientific Institution Basal Research Fund for Chinese Academy of Tropical Agricultural Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/SC/C9SC02474C

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1. Therapeutic design of peptide modulators of protein-protein interactions in membranes

2. MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria

3. End-to-end conformational communication through a synthetic purinergic receptor by ligand-induced helicity switching

4. An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein-Protein Interactions

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