Molecular mimicry: HUWE1 binds an atypical site in MIZ1 by adopting a typical BTB fold

Anushweta Asthana; Seth M Rubin

doi:10.1016/j.str.2021.10.005

Molecular mimicry: HUWE1 binds an atypical site in MIZ1 by adopting a typical BTB fold

Structure. 2021 Nov 4;29(11):1217-1218. doi: 10.1016/j.str.2021.10.005.

Authors

Anushweta Asthana¹, Seth M Rubin²

Affiliations

¹ Department of Chemistry and Biochemistry, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.
² Department of Chemistry and Biochemistry, University of California, Santa Cruz, Santa Cruz, CA 95064, USA. Electronic address: srubin@ucsc.edu.

PMID: 34739823
DOI: 10.1016/j.str.2021.10.005

Abstract

In this issue of Structure, Orth et al. describe an exposed binding site in the MIZ1 BTB domain due to an atypical flexible region within the BTB core. This site allows HECT-type ubiquitin ligase 1 to bind the MIZ1 homodimer by forming β strands and completing the canonical BTB fold.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Molecular Mimicry*
Protein Binding
Protein Conformation, beta-Strand
Ubiquitin / metabolism
Ubiquitin-Protein Ligases* / metabolism

Substances

Ubiquitin
Ubiquitin-Protein Ligases

Abstract

Publication types

MeSH terms

Substances

Grants and funding