Article
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction.
The Biochemical journal - 14 Dec 2009
Fuchs Margit, Poirier Dominic J, Seguin Samuel J, Lambert Herman, Carra Serena, Charette Steve J, Landry Jacques
Abstract excerpt
The molecular chaperone HspB8 [Hsp (heat-shock protein) B8] is member of the B-group of Hsps. These proteins bind to unfolded or misfolded proteins and protect them from aggregation. HspB8 has been reported to form a stable molecular complex with the chaperone cohort protein Bag3 (Bcl-2-associated athanogene 3). In the present study we identify the binding regions in HspB8 and Bag3 crucial for their interaction....
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