hsp90: twist and fold.
review · Level V
Where this comes from
- Record sourced from PubMed, PMID 17055424.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
Molecular chaperones are cellular machines that facilitate protein folding. The crystal structures of HtpG, the Escherichia coli homolog of hsp90, reported in this issue (Shiau et al., 2006) together with the recently published structures of an hsp90-cochaperone complex (Ali et al., 2006) and an hsp90-client protein complex (Vaughan et al., 2006), reveal exciting insights into the hsp90 reaction cycle.
Medical subject headings
- Adenine Nucleotides
- Escherichia coli Proteins
- HSP90 Heat-Shock Proteins
- Models, Molecular