Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Ligand Binding Sites

Ligand Binding Sites

Ligand Binding and Linkage

Ligand Binding and Linkage

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...

Ligand Binding and Linkage

Ligand Binding and Linkage

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

Conserved Binding Sites

Conserved Binding Sites

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...

You might also read

Related Articles

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

Sort by

Same author

Nonspecific Cellular Interactions Are a Key Determinant in the Disposition of Fc-Fused Proteins.

Molecular pharmaceutics·2026

Same author

Autonomous IL-36R signaling in neutrophils activates potent antitumor effector functions.

The Journal of clinical investigation·2023

Same author

Protein production from HEK293 cell line-derived stable pools with high protein quality and quantity to support discovery research.

PloS one·2023

Same author

VERITAS: Harnessing the power of nomenclature in biologic discovery.

mAbs·2023

Same author

Toward generalizable prediction of antibody thermostability using machine learning on sequence and structure features.

mAbs·2023

Same author

Author Correction: Development of spirulina for the manufacture and oral delivery of protein therapeutics.

Nature biotechnology·2022

Same journal

Breaking the Stability-Activity-Selectivity Trilemma in Unspecific Peroxygenase through Computation-Based Cross-Regional Combinatorial Mutagenesis.

ACS synthetic biology·2026

Same journal

Sequential Plasmid Curing and Genome Editing in <i>Escherichia coli</i> Nissle 1917.

ACS synthetic biology·2026

Same journal

An Explainable Deep Learning Framework Integrating DNA Sequence and Transcription Initiation Signals for Gene Expression Prediction.

ACS synthetic biology·2026

Same journal

A Multitask Prediction Framework for CircRNAs, Drugs, and Diseases Based on Multi-View Information Integration and Graph Contrastive Learning.

ACS synthetic biology·2026

Same journal

Engineering Modular Cargo Loading Strategies for Carboxysome-Derived Protein Particles.

ACS synthetic biology·2026

Same journal

Suppression of Salmonella Effectors with CRISPRi Controls the Immune Response to Bacterial Therapies.

ACS synthetic biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Feb 5, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Engineered Biosensors from Dimeric Ligand-Binding Domains.

Benjamin W Jester^1,2, Christine E Tinberg³, Matthew S Rich²

¹Howard Hughes Medical Institute , University of Washington , Seattle , Washington 98195 , United States.

ACS Synthetic Biology

|September 12, 2018

Summary

This summary is machine-generated.

We developed advanced Saccharomyces cerevisiae biosensors using destabilized dimeric ligand-binding domains. These engineered biosensors show improved dynamic range and sensitivity for synthetic biology applications.

Keywords:

biosensor directed evolution ligand-binding domain logic gate next generation sequencing protein engineering transcription factor

More Related Videos

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Related Experiment Videos

Last Updated: Feb 5, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Area of Science:

Synthetic biology
Metabolic engineering
Biosensor development

Background:

Biosensors are crucial tools in synthetic biology and metabolic engineering.
Existing biosensors often require optimization for dynamic range and specificity.

Purpose of the Study:

To engineer a second generation of Saccharomyces cerevisiae biosensors with enhanced performance.
To improve biosensor dynamic range, sensitivity, and selectivity through protein engineering.

Main Methods:

Utilized destabilized dimeric ligand-binding domains that stabilize upon ligand binding.
Introduced destabilizing mutations at the dimer interface to increase dynamic range.
Employed computational redesign and functional selection to create improved heterodimeric biosensors.
Investigated mutations for enhanced sensitivity and selectivity to specific ligands.

Main Results:

Achieved an order of magnitude increase in biosensor dynamic range via destabilizing mutations.
Developed heterodimeric biosensors with further enhanced dynamic range.
Demonstrated a synthetic "AND"-gate function with a digoxigenin and progesterone biosensor.
Identified mutations that improve biosensor sensitivity and selectivity for chemically similar ligands.

Conclusions:

The second-generation dimerizing biosensors offer increased flexibility for constructing biological logic gates.
These engineered biosensors provide powerful tools for advanced synthetic biology and metabolic engineering applications.
Further optimization of biosensor sensitivity and selectivity is achievable through targeted protein engineering.