title: Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state.
abstract: Hsc70 is the constitutively expressed mammalian heat shock 70 kDa (Hsp70) cytosolic chaperone. It plays a central role in cellular proteostasis and protein trafficking. Here, we present the backbone and methyl group assignments for the 386-residue nucleotide binding domain of the human protein. This domain controls the chaperone's allostery, binds multiple co-chaperones and is the target of several classes of known chemical Hsp70 inhibitors. The NMR assignments are based on common triple resonance experiments with triple labeled protein, and on several15N and13C-resolved 3D NOE experiments with methyl-reprotonated samples. A combination of computer and manual data interpretation was used.
authors.affiliation: Department of Biological Chemistry, The University of Michigan Medical School, 1500 Medical Center Drive, Ann Arbor, MI, 48109, USA. zuiderwe@umich.edu.
authors.forename: Erik R P
authors.initials: ER
authors.lastname: Zuiderweg
authors.affiliation: Institute for Neurodegenerative Disease, University of California at San Francisco, 675 Nelson Rising Lane, San Francisco, CA, 94158, USA.
authors.forename: Jason E
authors.initials: JE
authors.lastname: Gestwicki
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072417:Protein Domains
chemical_list: D018840:HSP70 Heat-Shock Proteins; D000244:Adenosine Diphosphate
keywords: Automatic assignments; Chaperones; Hsp70; Methyl reprotonation