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

Mapping of the auto-inhibitory interactions of protein kinase R by nuclear magnetic resonance.

Journal of molecular biology - 1 Dec 2006

Gelev Vladimir, Aktas Huseyin, Marintchev Assen, Ito Takuhiro, Frueh Dominique, Hemond Michael, Rovnyak David, Debus Mirijam, Hyberts Sven, Usheva Anny, Halperin Jose, Wagner Gerhard

Abstract excerpt

The dsRNA-dependent protein kinase (PKR) is a key mediator of the anti-viral and anti-proliferative effects of interferon. Unphosphorylated PKR is characterized by inhibitory interactions between the kinase and RNA binding domains (RBDs), but the structural details of the latent state and its unraveling during activation are not well understood. To study PKR regulation by NMR we assigned a large portion of the...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to eIF-2 Kinase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Eukaryotic Initiation Factor-2

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Phosphorylation

Share to Protein Conformation

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 17011579
DOI: 10.1016/j.jmb.2006.08.077
PMCID: PMC3622519

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping of the auto-inhibitory interactions of protein kinase R by nuclear magnetic resonance.PMID 17011579Read ↗

Human noncoding RNA 886 (nc886) adopts two structurally distinct conformers that are functionally opposing regulators of PKR.Semantic proximity Read ↗

Mechanism of PKR activation: dimerization and kinase activation in the absence of double-stranded RNA.Semantic proximity Read ↗

Site-specific modification and RNA crosslinking of the RNA-binding domain of PKR.Semantic proximity Read ↗

Phosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity.Semantic proximity Read ↗

Mutational analysis of the double-stranded RNA (dsRNA) binding domain of the dsRNA-activated protein kinase, PKR.Semantic proximity Read ↗

Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop.Semantic proximity Read ↗

Limited Proteolysis Combined with Stable Isotope Labeling Reveals Conformational Changes in Protein (Pseudo)kinases upon Binding Small Molecules.Semantic proximity Read ↗

Molecular basis for PKR activation by PACT or dsRNA.Semantic proximity Read ↗

Viral dsRNA Inhibitors Prevent Self-association and Autophosphorylation of PKRSemantic proximity Read ↗

PKR activity modulation by phosphomimetic mutations of serine residues located three aminoacids upstream of double-stranded RNA binding motifs.Semantic proximity Read ↗

Requirement for kinase-induced conformational change in eukaryotic initiation factor 2alpha (eIF2alpha) restricts phosphorylation of Ser51.Semantic proximity Read ↗

Determination of the human type I interferon receptor binding site on human interferon‐α2 by cross saturation and an NMR‐based model of the complexSemantic proximity Read ↗

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