Ontology highlight
ABSTRACT:
SUBMITTER: Page RC
PROVIDER: S-EPMC3370901 | biostudies-literature | 2012 Jun
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology and crystallization communications 20120523 Pt 6
Bag2, an atypical member of the Bag family of Hsp70 co-chaperones, acts as both an Hsp70 nucleotide-exchange factor and an inhibitor of the Hsp70-binding E3 ubiquitin ligase CHIP (carboxyl-terminus of Hsp70-interacting protein). The amino-terminal domain of Bag2 (Bag2-NTD), which is required for inhibition of CHIP, has no sequence homologs in the PDB. Native and selenomethionyl (SeMet) forms of Bag2-NTD were crystallized by hanging-drop vapor diffusion. Native Bag2-NTD crystals diffracted to 2.2 ...[more]