Noncovalent dimerization of ubiquitin

Angew Chem Int Ed Engl. 2012 Jan 9;51(2):469-72. doi: 10.1002/anie.201106190. Epub 2011 Nov 23.

Abstract

Another kind of dynamics: Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5 mM. The two subunits adopt an array of relative orientations, utilizing an interface also for binding to other proteins (see picture). Quaternary fluctuation among members of the dimer ensemble constitutes a different kind of dynamics that complements the tertiary dynamics of each ubiquitin subunit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Kinetics
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Multimerization*
  • Ubiquitin / chemistry*

Substances

  • Ubiquitin