Abstract
Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70 chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within substrates provide insights into the principles governing Hsp70 interaction with polypeptide chains. DnaK recognizes extended peptide strands composed of up to five consecutive hydrophobic residues within and positively charged residues outside the substrate binding cavity.
| Original language | English |
|---|---|
| Pages (from-to) | 342-349 |
| Number of pages | 8 |
| Journal | Nature Structural Biology |
| Volume | 4 |
| Issue number | 5 |
| Publication status | Published - 1 May 1997 |
| Externally published | Yes |
Keywords
- adenosine triphosphatase
- adenosine triphosphate
- bacterial protein
- chaperone
- heat shock protein 70
- polypeptide
- binding site
- enzyme substrate
- Escherichia coli
- molecular model
- nonhuman
- priority journal
- protein binding
- protein folding
- protein protein interaction
- review