Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone

The molecular chaperone heat shock protein 70 (Hsp70) plays a vital role in cellular processes, including protein folding and assembly, and helps prevent aggregation under physiological and stress-related conditions. Although the structural changes undergone by full-length client proteins upon inter...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2015-08, Vol.112 (31), p.E4206-E4215
Hauptverfasser:	Lee, Jung Ho, Zhang, Dongyu, Hughes, Christopher, Okuno, Yusuke, Sekhar, Ashok, Cavagnero, Silvia
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate - metabolism Animals Biological Sciences Drosophila melanogaster Drosophila Proteins - chemistry Drosophila Proteins - metabolism E coli Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Heat shock proteins HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - metabolism Magnetic Resonance Spectroscopy Models, Biological Molecular Chaperones - chemistry Molecular Chaperones - metabolism Molecules PNAS Plus Protein Binding Protein Conformation Protein Folding Solvents src Homology Domains Substrate Specificity
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