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

Probing the determinants of diacylglycerol binding affinity in the C1B domain of protein kinase Cα.

Journal of molecular biology - 20 May 2011

Stewart Mikaela D, Morgan Brittany, Massi Francesca, Igumenova Tatyana I

Abstract excerpt

C1 domains are independently folded modules that are responsible for targeting their parent proteins to lipid membranes containing diacylglycerol (DAG), a ubiquitous second messenger. The DAG binding affinities of C1 domains determine the threshold concentration of DAG required for the propagation of signaling response and the selectivity of this response among DAG receptors in the cell. The structural...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Diglycerides

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

Share to Molecular Dynamics Simulation

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Conformation

Share to Protein Kinase C-alpha

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 21419781
DOI: 10.1016/j.jmb.2011.03.020
PMCID: PMC3489171

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

Probing the determinants of diacylglycerol binding affinity in the C1B domain of protein kinase Cα.PMID 21419781Read ↗

Structure of membrane diacylglycerol kinase in lipid bilayers.Semantic proximity Read ↗

Crystal structure and allosteric activation of protein kinase C βII.Semantic proximity Read ↗

Electrostatic and hydrophobic interactions differentially tune membrane binding kinetics of the C2 domain of protein kinase Cα.Semantic proximity Read ↗

Molecular dynamics simulations corroborate recombinant expression studies carried out on three αIIb β-propeller mutations reported in Indian Glanzmann thrombasthenia patients.Semantic proximity Read ↗

Dynamic Allostery in PLCγ1 and Its Modulation by a Cancer Mutation Revealed by MD Simulation and NMR.Semantic proximity Read ↗

Expression and purification of the N-terminal regulatory domain of Protein Kinase C for biophysical studies.Semantic proximity Read ↗

Structural Basis of Protein Kinase Cα Regulation by the C-Terminal Tail.Semantic proximity Read ↗

The D75N and P161S Mutations in the C0-C2 Fragment of cMyBP-C Associated with Hypertrophic Cardiomyopathy Disturb the Thin Filament Activation, Nucleotide Exchange in Myosin, and Actin-Myosin Interaction.Semantic proximity Read ↗

Mechanistic and evolutionary insights into isoform-specific ‘supercharging’ in DCLK family kinasesSemantic proximity Read ↗

The Role of Regulatory Domains in Maintaining Autoinhibition in the Multidomain Kinase PKCα.Semantic proximity Read ↗

The origin of C1A-C2 interdomain interactions in protein kinase Calpha.Semantic proximity Read ↗

Distinct structural mechanisms determine substrate affinity and kinase activity of protein kinase Cα.Semantic proximity Read ↗

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