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Related Concept Videos

Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: Jul 12, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Tyrosine kinases sample unique activation ensembles.

Yanchen Zhu, Matteo T Degiacomi, Antonia S J S Mey

    Biorxiv : the Preprint Server for Biology
    |July 10, 2026
    PubMed
    Summary
    This summary is machine-generated.

    Protein kinase activation involves complex conformational changes. This study reveals distinct activation pathways for ABL1, EGFR, and MET kinases, challenging universal mechanism assumptions and highlighting new inhibitor design targets.

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    Last Updated: Jul 12, 2026

    Identification of Kinase-substrate Pairs Using High Throughput Screening
    11:13

    Identification of Kinase-substrate Pairs Using High Throughput Screening

    Published on: August 29, 2015

    Assaying Protein Kinase Activity with Radiolabeled ATP
    08:05

    Assaying Protein Kinase Activity with Radiolabeled ATP

    Published on: May 26, 2017

    Monitoring Kinase and Phosphatase Activities Through the Cell Cycle by Ratiometric FRET
    13:38

    Monitoring Kinase and Phosphatase Activities Through the Cell Cycle by Ratiometric FRET

    Published on: January 27, 2012

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Computational Biology

    Background:

    • Protein kinase activation is crucial for cellular signaling.
    • Conformational changes, including the Asp-Phe-Gly (DFG) motif, drive kinase activity.
    • The universality of kinase activation mechanisms remains an open question.

    Purpose of the Study:

    • To compare the conformational landscapes and activation mechanisms of ABL1, EGFR, and MET kinase domains.
    • To investigate whether kinase activation follows a universal pathway.

    Main Methods:

    • Utilized over 8.3 milliseconds of unbiased molecular dynamics simulations.
    • Employed Markov state models (MSMs) to analyze conformational dynamics.
    • Applied a transfer seeding strategy with AlphaFold2 models to explore uncharacterized conformational states.

    Main Results:

    • Identified distinct kinetic networks for related DFG-motif geometries.
    • Revealed kinase-specific activation pathways connecting shared structural states.
    • Demonstrated that different regulatory elements control the slowest activation step across kinases.

    Conclusions:

    • Kinase activation mechanisms are not universal, despite shared nomenclature.
    • Distinct transition pathways exist between different kinase domains.
    • Identified novel regions critical for kinase activity and potential inhibitor design.