The Extent of Extended-Ubiquitin Binding to the Proteasome

Jeroen Roelofs

doi:10.1016/j.str.2020.04.013

The Extent of Extended-Ubiquitin Binding to the Proteasome

Structure. 2020 May 5;28(5):489-491. doi: 10.1016/j.str.2020.04.013.

Author

Jeroen Roelofs¹

Affiliation

¹ Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Blvd, Kansas City, KS 66160, USA. Electronic address: jroelofs@kumc.edu.

PMID: 32375056
DOI: 10.1016/j.str.2020.04.013

Abstract

In this issue of Structure, Lu et al. (2020) describe an NMR-based study showing the proteasome ubiquitin receptor hRpn13 bound to an extended conformation of K48-diubiquitin that is different from previously described structures of K48-diubiquitin. Observed dynamic binding properties suggest an ability of substrates to hop between proteasome ubiquitin receptors.

Publication types

Comment

MeSH terms

Molecular Conformation
Proteasome Endopeptidase Complex*
Protein Binding
Ubiquitin*
Ubiquitins

Substances

Ubiquitin
Ubiquitins
Proteasome Endopeptidase Complex

Grants and funding

R01 GM118660/GM/NIGMS NIH HHS/United States