Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. - Wikidata - awgldk - TriplyDB

Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.

Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.

http://www.wikidata.org/entity/Q35847276

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Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Insights into the molecular mechanism of allostery in Hsp70s.DNAJs: more than substrate delivery to HSPA Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions The ensemble nature of allostery NMR insights into protein allostery Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 Structural Basis of J Cochaperone Binding and Regulation of Hsp70 Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket Substrate-binding domain conformational dynamics mediate Hsp70 allostery Allostery in the Hsp70 chaperone proteins Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP Identification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaK Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins Allostery in Hsp70 chaperones is transduced by subdomain rotations The HSP70 chaperone machinery: J proteins as drivers of functional specificity Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes.Kinks, loops, and protein folding, with protein A as an example.Pathways of allosteric regulation in Hsp70 chaperones.Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove.Small molecule DnaK modulators targeting the beta-domain.Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.Molecular dynamics reveal the essential role of linker motions in the function of cullin-RING E3 ligases Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly.Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocation Kinetic and structural characterization of human mortalin The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.

P2860

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P2860

Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.

http://www.wikidata.org/entity/Q35847276

description

2007 nî lūn-bûn

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2007年の論文

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Hsp70 chaperone ligands contro ...... ted by the interdomain linker.

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Hsp70 chaperone ligands contro ...... ted by the interdomain linker.

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J.MOLCEL.2007.02.020

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Hsp70 chaperone ligands contro ...... ted by the interdomain linker.

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P2093

Diana L Montgomery

http://www.w3.org/2001/XMLSchema#string

Gizem Dinler

http://www.w3.org/2001/XMLSchema#string

Joanna F Swain

http://www.w3.org/2001/XMLSchema#string

Lila M Gierasch

http://www.w3.org/2001/XMLSchema#string

Mathias Stotz

http://www.w3.org/2001/XMLSchema#string

Renuka Sivendran

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P2860

Hsp70 chaperones: cellular functions and molecular mechanism

Structural insights into substrate binding by the molecular chaperone DnaK

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

Molecular chaperones and protein quality control

Pathways of chaperone-mediated protein folding in the cytosol

Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.

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27-39

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10.1016/J.MOLCEL.2007.02.020

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1

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26

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17434124

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molecular chaperones

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1894942

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