Solution Structure of BAG Domains: BAG1dN
EMSL Project ID
2143
Abstract
BAG1 is a novel multifunctional protein first identified as a molecule that binds to the anti-apoptotic protein Bcl-2. With the discovery that BAG1 binds tightly to heat shock proteins Hsc70/Hsp70, it became clear that the BAG family of regulators modulate responses to cell death or cell stress through protein-protein interactions. The sequence of the conserved BAG domain, contained in all members of the family, is not homologous with other known proteins and thus is predicted to assume a novel 3D folding pattern. We are using NMR methods to study a fragment of BAG1 that is well-ordered and129 residues in length. With data recorded at EMSL in a previous cycle on the 750 MHz spectrometer, vitually complete HN, N, Calpha, Cbeta, C' and Halpha assignements have been made, and backbone dynamics and chemical shift index analyses indicated the helical regions. The highly helical BAG protein binds to Hsc70 and the next step is to study the binding interactions between 15N,2H-labeled BAG1dN (15 Kd) complexed with unlabeled Hsc70 ATPase domain (45Kd).Comparison of the shifts in the free and bound form will localize the binding interface and map contact residues on BAG1. Time was awarded in the previous cycle however our scheduled dates have not come yet. We anticipate that more high field experiments will be needed in the coming cycle, for example for TROSY, CRINEPT and cross-saturation experiments. We request one week on the 800 MHz spectrometer for these measurements.
Project Details
Project type
Capability Research
Start Date
2001-07-25
End Date
2001-10-02
Status
Closed
Released Data Link
Team
Principal Investigator