Mode of inhibitory binding of epigallocatechin gallate to the ubiquitin-activating enzyme Uba1 via accelerated molecular dynamics-Reference-Cited by-同舟云学术

Mode of inhibitory binding of epigallocatechin gallate to the ubiquitin-activating enzyme Uba1 via accelerated molecular dynamics

Published:2021 Issue:14 Volume:11 Page:8264-8276
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Gaur Paras¹²³⁴⁵^ORCID,Fenteany Gabriel¹²³⁴,Tyagi Chetna⁵⁶⁷⁸⁴^ORCID

Affiliation:

1. Institute of Genetics

2. Biological Research Centre

3. 6726 Szeged

4. Hungary

5. Doctoral School of Biology

6. Faculty of Sciences and Informatics

7. University of Szeged

8. Szeged

Abstract

The hinge-like movement of the SCCH domain upon ligand binding closes the ubiquitin binding site and disrupts the interfaces crucial for thioester bond formation.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/RA/D0RA09847G

Reference42 articles.

1. Multilevel structure–activity profiling reveals multiple green tea compound families that each modulate ubiquitin-activating enzyme and ubiquitination by a distinct mechanism

2. Robust high-throughput assays to assess discrete steps in ubiquitination and related cascades

3. Development of inhibitors in the ubiquitination cascade

4. Ubiquitin Ligases: Structure, Function, and Regulation

5. Emerging drug development technologies targeting ubiquitination for cancer therapeutics

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