ArticleMolecular systems biology2010
An interdomain sector mediating allostery in Hsp70 molecular chaperones.
Article in Molecular systems biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 128 citations in OpenAlex.
- Protein Surface Site Determines the Evolutionary Accessibility of Allosteric Regulation.bioRxiv : the preprint server for biology · 2026Article
- Coevolving residues distant from the ligand binding site are involved in GAF domain function.Communications chemistry · 2025Article
- Engineering Proteins Using Statistical Models of Coevolutionary Sequence Information.Cold Spring Harbor perspectives in biology · 2024Review
- Knowledge-guided data mining on the standardized architecture of NRPS: Subtypes, novel motifs, and sequence entanglements.PLoS computational biology · 2023Article
- Article
- Extracting phylogenetic dimensions of coevolution reveals hidden functional signals.Scientific reports · 2022Article
- Coevolutionary methods enable robust design of modular repressors by reestablishing intra-protein interactions.Nature communications · 2021Article
- Structural Communication between theInternational journal of molecular sciences · 2021Article
- The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021Review
- RNA sectors and allosteric function within the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones.The Journal of biological chemistry · 2019Review
- A Local Allosteric Network in Heat Shock Protein 70 (Hsp70) Links Inhibitor Binding to Enzyme Activity and Distal Protein-Protein Interactions.ACS chemical biology · 2018Article
- Engineering allosteric regulation in protein kinases.Science signaling · 2018Article
- Coevolving residues inform protein dynamics profiles and disease susceptibility of nSNVs.PLoS computational biology · 2018Article
- Co-evolution networks of HIV/HCV are modular with direct association to structure and function.PLoS computational biology · 2018Article
- Advances in bioluminescence imaging: new probes from old recipes.Current opinion in chemical biology · 2018Review
- Intra-molecular pathways of allosteric control in Hsp70s.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- An evolutionary hotspot defines functional differences between CRYPTOCHROMES.Nature communications · 2018Article
- Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Allosteric coupling between protein domains is fundamental to many cellular processes. For example, Hsp70 molecular chaperones use ATP binding by their actin-like N-terminal ATPase domain to control substrate interactions in their C-terminal substrate-binding domain, a reaction that is critical for protein folding in cells. Here, we generalize the statistical coupling analysis to simultaneously evaluate co-evolution between protein residues and functional divergence between sequences in protein sub-families. Applying this method in the Hsp70/110 protein family, we identify a sparse but structurally contiguous group of co-evolving residues called a 'sector', which is an attribute of the allosteric Hsp70 sub-family that links the functional sites of the two domains across a specific interdomain interface. Mutagenesis of Escherichia coli DnaK supports the conclusion that this interdomain sector underlies the allosteric coupling in this protein family. The identification of the Hsp70 sector provides a basis for further experiments to understand the mechanism of allostery and introduces the idea that cooperativity between interacting proteins or protein domains can be mediated by shared sectors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.