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Cited by 253

The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.

An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones

Open access
Zhuravleva, Anastasia, Clerico, Eugenia M., Gierasch, Lila M.·2012·Cell
DOI 10.1016/j.cell.2012.11.002
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Abstract

Summary The allosteric mechanism of Hsp70 molecular chaperones enables ATP binding to the N-terminal nucleotide-binding domain (NBD) to alter substrate affinity to the C-terminal substrate-binding domain (SBD), and substrate binding to enhance ATP hydrolysis. Cycling between ATP-bound and ADP-/substrate-bound states requires Hsp70s to visit a state with high ATPase activity and fast on/off kinetics of substrate binding. We have trapped this ‘allosterically active’ state for the E. coli Hsp70, DnaK, and identified how interactions between the NBD, the β-subdomain of the SBD, the SBD α-helical lid, and the conserved hydrophobic interdomain linker enable allosteric signal transmission between ligand-binding sites. Allostery in Hsp70s results from an energetic tug-of-war between domain conformations and formation of two orthogonal interfaces (between the NBD and SBD, and between the helical lid and the SBD). The resulting energetic tension underlies Hsp70 functional properties and enables them to be modulated by ligands and co-chaperones and ‘tuned’ through evolution.

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Metadata

Authors
Zhuravleva, A., Clerico, E. M., & Gierasch, L. M.
Venue
Cell
Publisher
Elsevier BV
Published
2012-12
Volume
151
Issue
6
Pages
1296-1307
ISSN
0092-8674 (ISSN-L)
DOI
10.1016/j.cell.2012.11.002
OpenAlex
W1999268424
Cited by
253
References
57
FWCI
8.71
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones. https://app.cochat.ai/papers/10.1016/j.cell.2012.11.002
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Zhuravleva, A., Clerico, E. M., & Gierasch, L. M. (2012). An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones. Cell. https://doi.org/10.1016/j.cell.2012.11.002

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.