期刊
FEBS LETTERS
卷 583, 期 21, 页码 3405-3411出版社
WILEY
DOI: 10.1016/j.febslet.2009.09.047
关键词
BAG-1; HSC70; HSP70; Interaction; Binding
资金
- Biotechnology and Biological Sciences Research Council
- Campaign and Cancer Research UK
BAG-1, a multifunctional protein, interacts with a plethora of cellular targets where the interaction with HSC70 and HSP70, is considered vital. Structural studies have demonstrated the C-terminal of BAG-1 forms a bundle of three alpha-helices of which helices 2 and 3 are directly involved in binding to the chaperones. Here we found peptides derived from helices 2 and 3 of BAG-1 interfered with BAG-1: HSC70 binding. We confirmed that a 12 amino-acid peptide from helix 2 directly interacted with HSC70 and when introduced into MCF-7 and ZR-75-1 cells, these peptides inhibited their growth. In conclusion, we have identified a small domain within BAG-1 which appears to play a critical role in the interaction with HSC70.
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