ArticleNature communications2017
Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
49 citing papers in PubMed, 76 citations in OpenAlex.
- A Small Molecule Substrate Mimic to Inhibit Bacterial Hsp70 Chaperone Function.Chembiochem : a European journal of chemical biology · 2026Article
- Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026Article
- Heat shock proteins (Hsp70 and Hsp90) in neurodegeneration: pathogenic roles and therapeutic potential.Frontiers in aging neuroscience · 2026Review
- Enhancing Cytosolic Internalization of [International journal of molecular sciences · 2025Article
- Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025Article
- Effects of Chromium Yeast Supplementation on SerumVeterinary sciences · 2025Article
- Exploring the Anticancer Potential of Proton Pump Inhibitors by Targeting GRP78 and V-ATPase: Molecular Docking, Molecular Dynamics, PCA, and MM-GBSA Calculations.International journal of molecular sciences · 2025Article
- Biochemical and biophysical characterization of Plasmodium falciparum glucose regulated protein 170.Scientific reports · 2025Article
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- A low-complexity linker as a driver of intra- and intermolecular interactions in DNAJB chaperones.Nature communications · 2025Article
- The structural and functional dynamics of BiP and Grp94: opportunities for therapeutic discovery.Trends in pharmacological sciences · 2025Review
- Single-molecule study of the dynamics of the molecular chaperone Hsp70 during the functional cycle.Biochemical Society transactions · 2025Review
- Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors.Nature communications · 2025Article
- Malate initiates a proton-sensing pathway essential for pH regulation of inflammation.Signal transduction and targeted therapy · 2024Article
- Targeted Analysis of Mitochondrial Protein Conformations and Interactions by Endogenous ROS-Triggered Cross-Linker Release.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis.Journal of molecular biology · 2024Review
- Identification of a druggable site on GRP78 at the GRP78-SARS-CoV-2 interface and virtual screening of compounds to disrupt that interface.Journal of computer-aided molecular design · 2024Article
- Article
- Elevated human placental heat shock protein 5 is associated with spontaneous preterm birth.Pediatric research · 2023Article
- Release of hepatitis B virions is positively regulated by glucose-regulated protein 78 through direct interaction with preS1.Journal of medical virology · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Cellular protein homeostasis depends on heat shock proteins 70 kDa (Hsp70s), a class of ubiquitous and highly conserved molecular chaperone. Key to the chaperone activity is an ATP-induced allosteric regulation of polypeptide substrate binding and release. To illuminate the molecular mechanism of this allosteric coupling, here we present a novel crystal structure of an intact human BiP, an essential Hsp70 in ER, in an ATP-bound state. Strikingly, the polypeptide-binding pocket is completely closed, seemingly excluding any substrate binding. Our FRET, biochemical and EPR analysis suggests that this fully closed conformation is the major conformation for the ATP-bound state in solution, providing evidence for an active release of bound polypeptide substrates following ATP binding. The Hsp40 co-chaperone converts this fully closed conformation to an open conformation to initiate productive substrate binding. Taken together, this study provided a mechanistic understanding of the dynamic nature of the polypeptide-binding pocket in the Hsp70 chaperone cycle.
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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.