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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...
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,...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: Jul 15, 2026

A Phenotyping Regimen for Genetically Modified Mice Used to Study Genes Implicated in Human Diseases of Aging
09:37

A Phenotyping Regimen for Genetically Modified Mice Used to Study Genes Implicated in Human Diseases of Aging

Published on: July 14, 2016

Interactions between important regulatory proteins and human alphaB crystallin.

Joy G Ghosh1, Ananth K Shenoy, John I Clark

  • 1Biomolecular Structure and Design, University of Washington, Seattle, Washington 98195-7420, USA.

Biochemistry
|May 10, 2007
PubMed
Summary

AlphaB crystallin interacts with key regulatory proteins like FGF-2 and VEGF, crucial for cell growth and differentiation. These interactions highlight alphaB crystallin's role as a chaperone, protecting proteins from stress-induced unfolding and aggregation.

Related Experiment Videos

Last Updated: Jul 15, 2026

A Phenotyping Regimen for Genetically Modified Mice Used to Study Genes Implicated in Human Diseases of Aging
09:37

A Phenotyping Regimen for Genetically Modified Mice Used to Study Genes Implicated in Human Diseases of Aging

Published on: July 14, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • AlphaB crystallin is a small heat shock protein involved in cellular processes.
  • Regulatory proteins like growth factors and caspases play critical roles in cell signaling and apoptosis.

Purpose of the Study:

  • To identify specific interactions between alphaB crystallin and 12 regulatory proteins.
  • To determine the functional significance of these interactions, particularly regarding chaperone activity.

Main Methods:

  • Protein pin arrays were used to screen interactions between alphaB crystallin peptides and regulatory proteins.
  • Chaperone assays were performed using full-length and synthetic alphaB crystallin peptides.

Main Results:

  • AlphaB crystallin strongly interacted with FGF-2, NGF-beta, VEGF, insulin, and beta-catenin.
  • Identified specific alphaB crystallin sequences responsible for these interactions.
  • Demonstrated alphaB crystallin's ability to protect FGF-2 and VEGF from aggregation.

Conclusions:

  • AlphaB crystallin exhibits chaperone activity, protecting proteins like FGF-2 and VEGF from unfolding and aggregation.
  • The identified interaction sequences suggest a dual role for alphaB crystallin in chaperone activity and regulating cell growth/differentiation.