Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU)

Lignende værker

• Solution Structure of the Iron−Sulfur Cluster Cochaperone HscB and Its Binding Surface for the Iron−Sulfur Assembly Scaffold Protein IscU
  af: Füzéry, Anna K., et al.
  Udgivet: (2008)
• Three hydrophobic amino acids in Escherichia coli HscB make the greatest contribution to the stability of the HscB-IscU complex
  af: Füzéry, Anna K, et al.
  Udgivet: (2011)
• Structure and Dynamics of the Iron-Sulfur Cluster Assembly Scaffold Protein IscU and its Interaction with the Cochaperone HscB,
  af: Kim, Jin Hae, et al.
  Udgivet: (2009)
• HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apo-ferredoxin in an ATP-dependent reaction
  af: Chandramouli, Kala, et al.
  Udgivet: (2006)
• Human Mitochondrial Chaperone (mtHSP70) and Cysteine Desulfurase (NFS1) Bind Preferentially to the Disordered Conformation, Whereas Co-chaperone (HSC20) Binds to the Structured Conformation of the Iron-Sulfur Cluster Scaffold Protein (ISCU)
  af: Cai, Kai, et al.
  Udgivet: (2013)