Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis.

Proceedings of the National Academy of Sciences of the United States of America - 9 Feb 2010

Grinthal Alison, Adamovic Ivana, Weiner Beth, Karplus Martin, Kleckner Nancy

Abstract excerpt

PR65 is the two-layered (alpha-alpha solenoid) HEAT-repeat (Huntingtin, elongation factor 3, a subunit of protein phosphatase 2A, PI3 kinase target of rapamycin 1) scaffold of protein phosphatase PP2A. Molecular dynamics simulations predict that, at forces expected in living systems, PR65 undergoes (visco-)elastic deformations in response to pulling/pushing on its ends. At lower forces, smooth global flexural and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Microscopy, Atomic Force

Share to Molecular Dynamics Simulation

Share to Protein Phosphatase 2

Share to Stress, Mechanical

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 20133745
DOI: 10.1073/pnas.0914073107
PMCID: PMC2823866

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis.PMID 20133745Read ↗

Effects of Mutations on Tandem-Repeat Proteins Conformation Mechanisms. Application to the Phosphatase PP2A.Semantic proximity Read ↗

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs.Semantic proximity Read ↗

An interdisciplinary study of the mechanical and dynamic properties of α-solenoid repeat proteinsSemantic proximity Read ↗

Cryo-EM Reveals the Mechanochemical Cycle of Reactive Full-length Human Dynein-1Semantic proximity Read ↗

Extended regulation interface coupled to the allosteric network and disease mutations in the PP2A-B56δ holoenzymeSemantic proximity Read ↗

Structural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerizationSemantic proximity Read ↗

Substrate recruitment via eIF2γ enhances catalytic efficiency of a holophosphatase that terminates the Integrated Stress ResponseSemantic proximity Read ↗

The cryoEM structure of the fibril-forming low-complexity domain of hnRNPA2 reveals distinct differences from pathogenic amyloid and shows how mutation converts it to the pathogenic formSemantic proximity Read ↗

How an intrinsically disordered regulatory subunit assembles a PP1:eIF2 complex.Semantic proximity Read ↗

Chaperone-driven entropic separation of amyloid nanofilament bundlesSemantic proximity Read ↗

Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities.Semantic proximity Read ↗

Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.