ArticlePLoS computational biology2010
Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.
Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Identifying a non-conserved site for achieving allosteric covalent inhibition of CECR2.Acta pharmacologica Sinica · 2025Article
- New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE.The Journal of biological chemistry · 2024Article
- Heat shock proteins and cancer: The FoxM1 connection.Biochemical pharmacology · 2023Review
- Protein Quality Control in Glioblastoma: A Review of the Current Literature with New Perspectives on Therapeutic Targets.International journal of molecular sciences · 2022Review
- Allosteric Inter-Domain Contacts in Bacterial Hsp70 Are Located in Regions That Avoid Insertion and Deletion Events.International journal of molecular sciences · 2022Article
- Heat Shock Proteins in Benign Prostatic Hyperplasia and Prostate Cancer.International journal of molecular sciences · 2022Review
- Evodiamine inhibits both stem cell and non-stem-cell populations in human cancer cells by targeting heat shock protein 70.Theranostics · 2021Article
- Autophagic Inhibition via Lysosomal Integrity Dysfunction Leads to Antitumor Activity in Glioma Treatment.Cancers · 2020Article
- Structural characterization and molecular dynamics simulations of the caprine and bovine solute carrier family 11 A1 (SLC11A1).Journal of computer-aided molecular design · 2019Article
- Discorhabdin N, a South African Natural Compound, for Hsp72 and Hsc70 Allosteric Modulation: Combined Study of Molecular Modeling and Dynamic Residue Network Analysis.Molecules (Basel, Switzerland) · 2019Article
- 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
- Disrupted Hydrogen-Bond Network and Impaired ATPase Activity in an Hsc70 Cysteine Mutant.Biochemistry · 2018Article
- Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication.PLoS computational biology · 2017Article
- Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy.Cell chemical biology · 2016Article
- Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Structure (London, England : 1993) · 2016Review
- Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.Chemical reviews · 2016Review
- The Role of Conformational Dynamics and Allostery in the Disease Development of Human Ferritin.Biophysical journal · 2015Article
- Comparative study of the effectiveness and limitations of current methods for detecting sequence coevolution.Bioinformatics (Oxford, England) · 2015Article
- Conformational dynamics of nonsynonymous variants at protein interfaces reveals disease association.Proteins · 2015Article
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3 authors.
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Abstract
Catalysis of ADP-ATP exchange by nucleotide exchange factors (NEFs) is central to the activity of Hsp70 molecular chaperones. Yet, the mechanism of interaction of this family of chaperones with NEFs is not well understood in the context of the sequence evolution and structural dynamics of Hsp70 ATPase domains. We studied the interactions of Hsp70 ATPase domains with four different NEFs on the basis of the evolutionary trace and co-evolution of the ATPase domain sequence, combined with elastic network modeling of the collective dynamics of the complexes. Our study reveals a subtle balance between the intrinsic (to the ATPase domain) and specific (to interactions with NEFs) mechanisms shared by the four complexes. Two classes of key residues are distinguished in the Hsp70 ATPase domain: (i) highly conserved residues, involved in nucleotide binding, which mediate, via a global hinge-bending, the ATPase domain opening irrespective of NEF binding, and (ii) not-conserved but co-evolved and highly mobile residues, engaged in specific interactions with NEFs (e.g., N57, R258, R262, E283, D285). The observed interplay between these respective intrinsic (pre-existing, structure-encoded) and specific (co-evolved, sequence-dependent) interactions provides us with insights into the allosteric dynamics and functional evolution of the modular Hsp70 ATPase domain.
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