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

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.8K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.8K
Allosteric Regulation01:08

Allosteric Regulation

63.8K
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...
63.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

9.1K
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...
9.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.7K
2.7K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.7K
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...
5.7K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

6.7K
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...
6.7K

You might also read

Related Articles

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

Sort by
Same author

Inositol Thiophosphates as Inhibitors of Mammalian, Plant, and Fungal Phytases.

ACS chemical biology·2026
Same author

Synthesis and characterization of cortinarins - cryptic cyclic peptides from mushrooms of the genus <i>Cortinarius</i>.

Chemical science·2026
Same author

Cryo-electron microscopy structures of human cone visual pigments.

Science (New York, N.Y.)·2026
Same author

Secondary Site Ligand for Integrin αVβ3 Enables Targeted mRNA Delivery.

Angewandte Chemie (International ed. in English)·2026
Same author

Ultrarapid MC1R protein and associated plumage color evolution in the domestic chicken.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Polyfluoroalkyl-Tagged Cell-Penetrating Peptide-Additives Enhance Intracellular Protein Delivery via Sustained Monomeric Lipid Interaction.

Angewandte Chemie (International ed. in English)·2026
Same journal

DeepDOX1: A Dual-Drive Framework Integrating Deep Learning and First-Principles Quantum Chemistry for Drug-Protein Affinity Prediction.

JACS Au·2026
Same journal

Catalyst-Controlled Regiodivergent C-H Olefination of Furanyl Carbamates through a Rational Approach.

JACS Au·2026
Same journal

Charting the Biosynthetic Landscape of Hybrid Polyketide-Nonribosomal Peptide-Specialized Lipids.

JACS Au·2026
Same journal

Valence-State-Dependent Surface Lattice Oxygen in CeO<sub>2</sub>‑Modified VPO Catalysts: Elucidating the Mechanism of <i>n</i>‑Butane Selective Oxidation to Maleic Anhydride.

JACS Au·2026
Same journal

Quantitative Insights into Pressure-Dependent Mass Transport and Reaction Kinetics in Electrochemical CO<sub>2</sub> Reduction.

JACS Au·2026
Same journal

3‑Methylthiopropionic Acid Kills Carbapenem-Resistant <i>Klebsiella pneumoniae</i> by Disrupting Membrane Integrity and Bioenergetics.

JACS Au·2026
See all related articles

Related Experiment Video

Updated: Feb 28, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

635

A Cryptic Pocket Allosterically Modulates Oligosaccharide Binding to DC-SIGN.

Jonathan Lefèbre1,2,3, Maurice Besch1,2,3, Marcelo Daniel Gamarra4,5

  • 1Department of Pharmaceutical Sciences, University of Vienna, Josef-Holaubek-Platz 2, Vienna 1090, Austria.

JACS Au
|February 27, 2026
PubMed
Summary
This summary is machine-generated.

Researchers discovered a hidden pocket in DC-SIGN, a key immune receptor. This pocket regulates how DC-SIGN binds to sugars, offering a new target for drug development.

Keywords:
C-type lectinDC-SIGNNMRallosterycryptic pocket

More Related Videos

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

1.0K
Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

9.2K

Related Experiment Videos

Last Updated: Feb 28, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

635
Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

1.0K
Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

9.2K

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Dendritic cell-specific intercellular adhesion molecule-3 grabbing non-integrin (DC-SIGN) is a C-type lectin receptor vital for immune responses.
  • It plays a critical role in pathogen recognition and immune modulation by antigen-presenting cells.

Purpose of the Study:

  • To identify and characterize a novel cryptic allosteric pocket in DC-SIGN.
  • To understand how this pocket influences glycan binding and receptor function.

Main Methods:

  • Molecular dynamics simulations
  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Cryogenic electron microscopy (cryo-EM)
  • Biochemical assays

Main Results:

  • A previously unrecognized cryptic allosteric pocket in DC-SIGN was identified and characterized.
  • Rotation of the gatekeeper residue M270 exposes this pocket, modulating glycan binding.
  • Mutations mimicking pocket occupancy altered the conformational equilibrium and oligosaccharide affinity.
  • A complex interplay between Ca2+ binding sites and glycan binding surfaces was revealed.

Conclusions:

  • A hierarchical allosteric mechanism in DC-SIGN enables selective tuning of glycan affinity.
  • The identified cryptic pocket represents a novel therapeutic target for modulating C-type lectin function.