The Carboxyl-Terminal Lobe of Hsc70 ATPase Domain Is Sufficient for Binding to BAG1

The molecular co-chaperone BAG1 and other members of the BAG family bind to Hsp70/Hsc70 heat shock proteins through a conserved BAG domain that interacts with the ATPase domain of the chaperone. BAG1 and other accessory proteins stimulate ATP hydrolysis and regulate the ATP-driven activity of the ch...

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Veröffentlicht in:	Biochemical and biophysical research communications 2001-12, Vol.289 (5), p.1099-1105
Hauptverfasser:	Brive, Lars, Takayama, Shinichi, Briknarová, Klára, Homma, Sachiko, Ishida, Stacie K., Reed, John C., Ely, Kathryn R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism apoptosis BAG family Binding Sites Carrier Proteins - metabolism DNA-Binding Proteins heat shock protein HSC70 Heat-Shock Proteins HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Humans In Vitro Techniques Models, Molecular molecular chaperones Molecular Chaperones - chemistry Molecular Chaperones - metabolism nucleotide exchange factor Protein Binding Protein Conformation Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Surface Plasmon Resonance Transcription Factors
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