title: 1H,15N and13C resonance assignments for free and IEEVD peptide-bound forms of the tetratricopeptide repeat domain from the human E3 ubiquitin ligase CHIP.
abstract: The ubiquitin ligase CHIP catalyzes covalent attachment of ubiquitin to unfolded proteins chaperoned by the heat shock proteins Hsp70/Hsc70 and Hsp90. CHIP interacts with Hsp70/Hsc70 and Hsp90 by binding of a C-terminal IEEVD motif found in Hsp70/Hsc70 and Hsp90 to the tetratricopeptide repeat (TPR) domain of CHIP. Although recruitment of heat shock proteins to CHIP via interaction with the CHIP-TPR domain is well established, alterations in structure and dynamics of CHIP upon binding are not well understood. In particular, the absence of a structure for CHIP-TPR in the free form presents a significant limitation upon studies seeking to rationally design inhibitors that may disrupt interactions between CHIP and heat shock proteins. Here we report the1H,13C, and15N backbone and side chain chemical shift assignments for CHIP-TPR in the free form, and backbone chemical shift assignments for CHIP-TPR in the IEEVD-bound form. The NMR resonance assignments will enable further studies examining the roles of dynamics and structure in regulating interactions between CHIP and the heat shock proteins Hsp70/Hsc70 and Hsp90.
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, 651 E. High St, Oxford, OH, 45056, USA.
authors.forename: Huaqun
authors.initials: H
authors.lastname: Zhang
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, 651 E. High St, Oxford, OH, 45056, USA.
authors.forename: Cameron
authors.initials: C
authors.lastname: McGlone
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, 651 E. High St, Oxford, OH, 45056, USA.
authors.forename: Matthew M
authors.initials: MM
authors.lastname: Mannion
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, 651 E. High St, Oxford, OH, 45056, USA. pagerc@miamioh.edu.
authors.forename: Richard C
authors.initials: RC
authors.lastname: Page
mesh_terms: D020816:Amino Acid Motifs; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism*; D000072417:Protein Domains; D020449:Repetitive Sequences, Amino Acid; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D009842:Oligopeptides; C467728:STUB1 protein, human; D044767:Ubiquitin-Protein Ligases
keywords: CHIP; Heat shock proteins; NMR; TPR; Ubiquitin ligase