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

Ligand Binding Sites02:40

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 Sites02:40

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...
Conserved Binding Sites01:49

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 analyses the...
Ligand Binding and Linkage00:49

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 the...
Ligand Binding and Linkage00:49

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 the...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...

You might also read

Related Articles

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

Sort by
Same author

Engineered protein nanoclusters reduce liver fibrosis and hepatocellular carcinoma in mice models.

Bioactive materials·2026
Same author

epiGPTope: A Machine Learning-Based Epitope Generator and Classifier.

ACS synthetic biology·2026
Same author

Magnetic nanoparticles as transducers for quick and direct virus detection in clinical samples.

Nanoscale·2025
Same author

Engineered Protein-Based Ionic Conductors for Sustainable Energy Storage Applications.

Advanced materials (Deerfield Beach, Fla.)·2025
Same author

Rational Crystal Contact Engineering for Programmable Self-Assembled Protein Architectures.

Angewandte Chemie (International ed. in English)·2025
Same author

SNUPN-Related Muscular Dystrophy: Novel Phenotypic, Pathological and Functional Protein Insights.

Annals of clinical and translational neurology·2025

Related Experiment Video

Updated: Jul 3, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

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

Published on: January 14, 2020

Ligand binding by repeat proteins: natural and designed.

Tijana Z Grove1, Aitziber L Cortajarena, Lynne Regan

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA. tijana.grove@yale.edu

Current Opinion in Structural Biology
|July 8, 2008
PubMed
Summary

Repeat proteins, with their modular design, offer unique surfaces for ligand binding. Recent advances explore their functional roles and engineered interactions with various molecules.

More Related Videos

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy
12:24

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy

Published on: September 29, 2016

Related Experiment Videos

Last Updated: Jul 3, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

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

Published on: January 14, 2020

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy
12:24

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy

Published on: September 29, 2016

Area of Science:

  • Structural biology
  • Protein engineering
  • Biochemistry

Background:

  • Repeat proteins are characterized by tandem arrays of small structural motifs.
  • This architecture results in non-globular, extended protein structures.
  • These structures provide large, highly specific surfaces for molecular interactions.

Purpose of the Study:

  • To review recent advances in understanding the functional role of repeat protein architecture.
  • To showcase natural repeat protein-ligand interactions.
  • To present examples of designed repeat protein-ligand interactions.

Main Methods:

  • Literature review of recent advances in repeat protein research.
  • Analysis of structural and functional data for natural repeat proteins.
  • Case studies of engineered repeat protein-ligand systems.

Main Results:

  • Repeat proteins' modularity enables specific ligand binding.
  • Diverse natural ligands interact with various repeat protein architectures.
  • Designed repeat proteins demonstrate tailored ligand-binding capabilities.

Conclusions:

  • The modular architecture of repeat proteins is key to their function.
  • Repeat proteins serve as versatile platforms for both natural and engineered molecular recognition.