Total chemical synthesis of the phosphorylated p62 UBA domain reveals that Ser407Pi but not Ser403Pi enhances ubiquitin binding-Reference-Cited by-同舟云学术

Total chemical synthesis of the phosphorylated p62 UBA domain reveals that Ser407Pi but not Ser403Pi enhances ubiquitin binding

Published:2020 Issue:42 Volume:18 Page:8709-8715
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Xu Ling¹²³⁴,Zhang Yan¹²³⁴,Li Yi-Ming⁵⁶³⁴,Lu Xian-Fu¹²³⁴^ORCID

Affiliation:

1. Department of Anesthesiology (High-Tech Branch)

2. the First Affiliated Hospital of Anhui Medical University

3. Hefei

4. China

5. School of Food and Biological Engineering

6. Hefei University of Technology

Abstract

Based on total chemical synthesis we prepared four types of phosphorylated p62 UBAs and found that phosphorylation at S407 but not at S403 enhanced the binding affinity between UBA and Ub.

Funder

The First Affiliated Hospital of Anhui Medical University

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/OB/D0OB01906B

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