Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity

Journal of Molecular Biology

Volumn 415, Issue 1, 2012, Pages 3-15

  Street, Timothy O ^a   Lavery, Laura A ^a   Verba, Kliment A ^a   Lee, Chung Tien ^b   Mayer, Matthias P ^b   Agard, David A ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

chaperone; Hsp90 mechanism; protein folding

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90; MONOMER;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION;

EID: 84855293594     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.10.038     Document Type: Article

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