Understanding β-strand mediated protein–protein interactions: tuning binding behaviour of intrinsically disordered sequences by backbone modification-Reference-Cited by-同舟云学术

Understanding β-strand mediated protein–protein interactions: tuning binding behaviour of intrinsically disordered sequences by backbone modification

Published:2024 Issue:26 Volume:15 Page:10237-10245
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Cawood Emma E.¹²^ORCID,Baker Emily³⁴,Edwards Thomas A.¹⁵⁶^ORCID,Woolfson Derek N.²³⁷^ORCID,Karamanos Theodoros K.⁸^ORCID,Wilson Andrew J.¹²⁹^ORCID

Affiliation:

1. Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, UK

2. School of Chemistry, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, UK

3. School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK

4. BrisSynBio, University of Bristol, Life Sciences Building, Tyndall Avenue, Bristol BS8 1TQ, UK

5. School of Molecular and Cellular Biology, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, UK

6. College of Biomedical Sciences, Larkin University, 18301 N Miami Ave #1, Miami, FL 33169, USA

7. School of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, UK

8. Department of Life Sciences, Imperial College London, London, SW7 2BX, UK

9. School of Chemistry, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK

Abstract

Systematic backbone N-methylation of a SIM peptide results in faster, tighter binging to SUMO driven by a reduced entropy of activation; this opens new opportunities to develop inhibitors of β-strand mediated protein–protein interactions.

Funder

Engineering and Physical Sciences Research Council

Biotechnology and Biological Sciences Research Council

Wellcome Trust

Leverhulme Trust

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D4SC02240H

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