Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface

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

Volumn 108, Issue 47, 2011, Pages 18966-18971

  Ahmad, Atta ^a,b   Bhattacharya, Akash ^a,c   McDonald, Ramsay A ^a   Cordes, Melissa ^a   Ellington, Benjamin ^a   Bertelsen, Eric B ^a,d   Zuiderweg, Erik R P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^d Enzo Life Sciences Inc   (United States)

Author keywords

Protein interactions; Structural biology

Indexed keywords

DISULFIDE; HEAT SHOCK PROTEIN 70; PROTEIN DNAJ; PROTEIN DNAK;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; MUTAGENESIS; NITROGEN NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; STOICHIOMETRY;

HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MULTIPROTEIN COMPLEXES; MUTAGENESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 82755187767     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111220108     Document Type: Article

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