Conformational selection in substrate recognition by Hsp70 chaperones

Moritz Marcinowski, Mathias Rosam, Christine Seitz, Johannes Elferich, Julia Behnke, Claudia Bello, Matthias J. Feige, Christian F.W. Becker, Iris Antes, Johannes Buchner

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


Hsp70s are molecular chaperones involved in the folding and assembly of proteins. They recognize hydrophobic amino acid stretches in their substrate binding groove. However, a detailed understanding of substrate specificity is still missing. Here, we use the endoplasmic reticulum-resident Hsp70 BiP to identify binding sites in a natural client protein. Two sites are mutually recognized and form stable Hsp70-substrate complexes. In silico and in vitro analyses revealed an extended substrate conformation as a crucial factor for interaction and show an unexpected plasticity of the substrate binding groove. The basic binding mechanism is conserved among different Hsp70s.

Original languageEnglish
Pages (from-to)466-474
Number of pages9
JournalJournal of Molecular Biology
Issue number3
StatePublished - 8 Feb 2013


  • BiP
  • Hsp70
  • Keywords
  • antibody
  • molecular chaperone
  • substrate conformation


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