Reply to Sousa et al.: Evaluation of competing J domain:Hsp70 complex models in light of methods used

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 13, 2012, Pages

  Zuiderweg, Erik R P ^a   Ahmad, Atta ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AUXILIN; HEAT SHOCK PROTEIN 70; PROTEIN DNAJ;

BINDING SITE; CRYSTAL STRUCTURE; DISULFIDE BOND; ESCHERICHIA COLI; HUMAN; LETTER; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN INTERACTION; SEQUENCE HOMOLOGY;

EID: 84859474741     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1121554109     Document Type: Letter

References (5)

1. Sousa R, et al. (2012) Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data. Proc Natl Acad Sci USA 109:E734.
2. Jiang J, et al. (2007) Structural basis of J cochaperone binding and regulation of Hsp70. Mol Cell 28:422-433. (Pubitemid 350030560)
3. Ahmad A, et al. (2011) Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface. Proc Natl Acad Sci USA 108:18966-18971.
4. Garimella R, et al. (2006) Hsc70 contacts helix III of the J domain from polyomavirus T antigens: Addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb. Biochemistry 45:6917-6929. (Pubitemid 43856676)
5. Jiang J, Prasad K, Lafer EM, Sousa R (2005) Structural basis of interdomain communication in the Hsc70 chaperone. Mol Cell 20:513-524. (Pubitemid 41668637)