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Cell. 2008 Jun 13;133(6):945-7. doi: 10.1016/j.cell.2008.05.036.

Swapping nucleotides, tuning Hsp70.

Author information

1
Department of Cell and Developmental Biology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. dmcyr@med.unc.edu

Abstract

Molecular chaperones such as heat shock protein 70 (Hsp70) are crucial for protein folding. Crystal structures of Hsp70 in a complex with the nucleotide exchange factor (NEF) Hsp110 reported in this issue of Cell (Polier et al., 2008) and in Molecular Cell (Schuermann et al., 2008) provide new insights into how NEF action specifies Hsp70 cellular function.

PMID:
18555768
PMCID:
PMC4445657
DOI:
10.1016/j.cell.2008.05.036
[Indexed for MEDLINE]
Free PMC Article

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