Ontology highlight
ABSTRACT:
SUBMITTER: Smith MC
PROVIDER: S-EPMC3856692 | biostudies-literature | 2013 Aug
REPOSITORIES: biostudies-literature
Smith Matthew C MC Scaglione K Matthew KM Assimon Victoria A VA Patury Srikanth S Thompson Andrea D AD Dickey Chad A CA Southworth Daniel R DR Paulson Henry L HL Gestwicki Jason E JE Zuiderweg Erik R P ER
Biochemistry 20130802 32
The E3 ubiquitin ligase CHIP (C-terminus of Hsc70 Interacting Protein, a 70 kDa homodimer) binds to the molecular chaperone Hsc70 (a 70 kDa monomer), and this complex is important in both the ubiquitination of Hsc70 and the turnover of Hsc70-bound clients. Here we used NMR spectroscopy, biolayer interferometry, and fluorescence polarization to characterize the Hsc70-CHIP interaction. We found that CHIP binds tightly to two molecules of Hsc70 forming a 210 kDa complex, with a Kd of approximately ...[more]