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.
MeSH terms
-
HSP110 Heat-Shock Proteins / chemistry
-
HSP110 Heat-Shock Proteins / metabolism
-
HSP70 Heat-Shock Proteins / chemistry*
-
HSP70 Heat-Shock Proteins / metabolism*
-
Humans
-
Models, Molecular
-
Protein Folding
-
Protein Structure, Tertiary
-
Saccharomyces cerevisiae / metabolism
-
Saccharomyces cerevisiae Proteins / chemistry
-
Saccharomyces cerevisiae Proteins / metabolism
Substances
-
HSP110 Heat-Shock Proteins
-
HSP70 Heat-Shock Proteins
-
SSE1 protein, S cerevisiae
-
Saccharomyces cerevisiae Proteins