Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

57.9K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
57.9K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.9K
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...
7.9K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

5.7K
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...
5.7K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K
The Two-State Receptor Model01:29

The Two-State Receptor Model

1.9K
The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with...
1.9K
Conserved Binding Sites01:49

Conserved Binding Sites

4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Spermidine in Alzheimer's Disease: Evidence from Animal Models and Human Studies.

Degenerative neurological and neuromuscular disease·2026
Same author

Synthesis of Methoxylated Benzoxanthones as Drug Metabolites of Antischistosomal Schistodiones-A Limited Environmental Risk.

Molecules (Basel, Switzerland)·2026
Same author

Gold-containing compounds target an apicomplexan Thioredoxin reductase: Disclosing reactivity through structural and functional characterization.

International journal of biological macromolecules·2026
Same author

The kidney and the balance of sulfur and nitrogen as fundamental components of pH homeostasis.

Physiological reports·2026
Same author

Unraveling in vitro phase separation and aggregation properties of the structured region of FMRP and the impact of Fragile X syndrome-linked mutations.

The FEBS journal·2026
Same author

Subjects Affected by Dementia with Lewy Bodies (DLB) and Multiple System Atrophy (MSA) Elevated Brain-Derived Neurotrophic Factor (BDNF) Serum Levels.

Current neuropharmacology·2026
Same journal

Evaluating the effect of γ-oryzanol on MASLD pathology using a medaka fish model.

FEBS open bio·2026
Same journal

Dose-dependent hepatotoxicity of hydrogen peroxide in HepG2 cells and its modulation by CYP450 induction.

FEBS open bio·2026
Same journal

How phagocytic cells kill bacteria: Lessons from a professional killer.

FEBS open bio·2026
Same journal

MagmaFlow: A desktop platform for artificial intelligence-driven expression analysis.

FEBS open bio·2026
Same journal

A new flow chip in combination with multiphoton microscopy as a protocol for longitudinal 3D imaging of tissue calcification under shear stress.

FEBS open bio·2026
Same journal

Effect of terahertz irradiation on DNA damage repair in living cells.

FEBS open bio·2026
See all related articles

Related Experiment Video

Updated: Jun 25, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

545

Is allostery a fuzzy concept?

Veronica Morea1, Francesco Angelucci2, Andrea Bellelli3

  • 1Institute of Molecular Biology and Pathology, CNR, Rome, Italy.

FEBS Open Bio
|May 24, 2024
PubMed
Summary
This summary is machine-generated.

Allostery, the regulation of protein function by ligands, has multiple definitions causing confusion. This review clarifies allosteric mechanisms and their mathematical descriptions for better understanding of protein regulation.

Keywords:
KNF modelMWC modelallosteryarginine repressorphosphoglycerate dehydrogenaseuracil phosphoribosyltransferase

More Related Videos

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.3K
Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells
09:20

Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells

Published on: July 6, 2021

2.4K

Related Experiment Videos

Last Updated: Jun 25, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

545
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.3K
Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells
09:20

Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells

Published on: July 6, 2021

2.4K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Allostery regulates crucial biological processes like catalysis and signal transduction.
  • Existing definitions of allostery are varied and often ambiguous, leading to conceptual confusion.
  • The precise definition and underlying mechanisms of allostery remain subjects of ongoing scientific discussion.

Purpose of the Study:

  • To review and clarify the diverse meanings of allostery in scientific literature.
  • To examine different protein reaction mechanisms associated with allosteric regulation.
  • To assign specific reaction mechanisms to proteins previously defined as allosteric.

Main Methods:

  • Literature review of allostery definitions and applications.
  • Analysis of protein reaction mechanisms, including concerted, induced-fit, and dissociation-association models.
  • Examination of experimental evidence for allosteric mechanisms in selected proteins.

Main Results:

  • Allostery is broadly defined by heterotropic ligand regulation and/or homotropic cooperativity.
  • Proteins exhibiting allostery encompass various mechanisms beyond the two-state concerted model.
  • Imprecise assignment of reaction mechanisms often contributes to the ambiguity surrounding allostery.

Conclusions:

  • A unified understanding of allosteric mechanisms requires precise definition and experimental validation.
  • Clarifying allosteric mechanisms enhances the study of protein function and regulation.
  • This review aims to reduce ambiguity in allostery research by examining specific protein examples.