Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data [Letters (Online Only)]
 

Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data [Letters (Online Only)]

Sousa, R., Jiang, J., Lafer, E. M., Hinck, A. P., Wang, L., Taylor, A. B., Maes, E. G....
Date: 2012-03-27

The work by Ahmad et al. (1) presented an NMR-based model for a bacterial DnaJ J domain:DnaK(Hsp70):ADP complex that differs from our crystal structure of a disulfide-linked bovine Hsc70:auxilin J domain complex (2). The work by Ahmad et al. (1) claimed that their model can better account for published mutational data, that their model is in better agreement with a previous NMR study of a bacterial DnaJ J domain:DnaK complex (3), and that the cross-link in our structure renders it irrelevant for understanding J domain:Hsp70 interactions or mechanism. However, bacterial DnaK and mammalian Hsc70 bind J proteins very differently. Bacterial... Read More


PNAS:
Number: 13
Volume: 109