@article{0269809136074b09a953690e496fdc38,
title = "Conformational selection in substrate recognition by Hsp70 chaperones",
abstract = "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.",
keywords = "BiP, Hsp70, Keywords, antibody, molecular chaperone, substrate conformation",
author = "Moritz Marcinowski and Mathias Rosam and Christine Seitz and Johannes Elferich and Julia Behnke and Claudia Bello and Feige, {Matthias J.} and Becker, {Christian F.W.} and Iris Antes and Johannes Buchner",
note = "Funding Information: We thank Ruoyu Sun for help with protein purification and measurements, Katja Baeuml for assistance with peptide synthesis and purification, and Martin Haslbeck for the DnaK proteins. We gratefully acknowledge funding provided by the Studienstiftung des deutschen Volkes (to M.M.), the German Academy of Sciences Leopoldina (grant number LPDS 2009-32 to M.J.F.), the Humboldt Foundation (to C.B.), and the Deutsche Forschungsgemeinschaft , the Fonds der Chemischen Industrie , and the Bayerische Forschungsstiftung (to J.B.). I.A. was supported by CIPSM Women . ",
year = "2013",
month = feb,
day = "8",
doi = "10.1016/j.jmb.2012.11.030",
language = "English",
volume = "425",
pages = "466--474",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",
}