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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

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Related Experiment Video

Updated: Jun 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

Modular composition predicts kinase/substrate interactions.

Yichuan Liu1, Aydin Tozeren

  • 1Center for Integrated Bioinformatics, Drexel University, Philadelphia, PA 19104, USA.

BMC Bioinformatics
|June 29, 2010
PubMed
Summary
This summary is machine-generated.

This study identifies domain patterns in kinases and substrates to predict phosphorylation events. The method accurately predicts kinase-substrate interactions, aiding in mapping cell signaling pathways.

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Last Updated: Jun 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

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Systems Biology

Background:

  • Phosphorylation events are crucial for cellular signaling and metabolism.
  • Existing knowledge of kinase-substrate interactions is incomplete.
  • Human protein sequences require comprehensive domain analysis for functional insights.

Purpose of the Study:

  • To identify domain composition patterns in kinases and their substrates.
  • To develop a predictive model for kinase-substrate binding events.
  • To enhance the annotation of cellular protein networks.

Main Methods:

  • Utilized the PROSITE domain annotation tool to scan human protein sequences.
  • Identified statistically enriched domain string pairs (signature pairs) in kinase-substrate couples.
  • Applied identified signature pairs to predict kinase-substrate interactions in a validation dataset.

Main Results:

  • Discovered signature pairs highly specific to distinct kinase subtypes.
  • Achieved high statistical accuracy in predicting kinase-substrate interactions using the developed method.
  • Validated the predictive power of signature pairs on an independent dataset.

Conclusions:

  • The developed method accurately predicts protein phosphorylation events with good coverage.
  • This approach significantly expands current understanding of cell signaling pathways.
  • The findings offer a valuable tool for developing combination therapies for complex diseases.