hsp90: twist and fold

Klaus Richter; Johannes Buchner

doi:10.1016/j.cell.2006.10.004

hsp90: twist and fold

Cell. 2006 Oct 20;127(2):251-3. doi: 10.1016/j.cell.2006.10.004.

Authors

Klaus Richter¹, Johannes Buchner

Affiliation

¹ Department of Chemistry, Technische Universität München, Germany.

PMID: 17055424
DOI: 10.1016/j.cell.2006.10.004

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.

Publication types

Comment

MeSH terms

Adenine Nucleotides / chemistry*
Adenine Nucleotides / metabolism
Binding Sites
Dimerization
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / metabolism
HSP90 Heat-Shock Proteins / chemistry*
HSP90 Heat-Shock Proteins / metabolism
Models, Molecular*
Protein Binding
Protein Conformation
Protein Folding

Substances

Adenine Nucleotides
Escherichia coli Proteins
HSP90 Heat-Shock Proteins
HtpG protein, E coli