Noncovalent dimerization of ubiquitin.

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.

SUBMITTER: Liu Z 

PROVIDER: S-EPMC3303887 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature