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

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

2.6K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
2.6K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.7K
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,...
5.7K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

6.9K
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
6.9K
Activation of Integrins01:15

Activation of Integrins

3.3K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
3.3K
Proteoglycans01:05

Proteoglycans

3.9K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

3.8K
The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
3.8K

You might also read

Related Articles

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

Sort by
Same author

High-Throughput Screening of Isomeric Reaction Products by Droplet Microfluidics Coupled to Cyclic Ion Mobility-Mass Spectrometry.

Analytical chemistry·2026
Same author

Chemical Probes to Reveal the Assembly and Dynamics of Wall Teichoic Acids.

Journal of the American Chemical Society·2026
Same author

Side-Chain-Based Cross-Linking of Amorphous Iono-Electronic Conductive Polymers for Thermo-Chemical Stability in Electrochemical Devices.

ACS applied materials & interfaces·2026
Same author

High-Throughput Discovery of Conformation-Switching Mechanophores with Enhanced Reactivity and Stability.

Inorganic chemistry·2026
Same author

Mechanophore cross-linking enhances ballistic energy dissipation of polymers.

Nature·2026
Same author

QuantumPDB: A Workflow for High-Throughput Quantum Cluster Model Generation from Protein Structures.

Journal of chemical information and modeling·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: Jun 14, 2025

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

3.3K

CH-π Interactions Are Required for Human Galectin-3 Function.

Roger C Diehl1, Rajeev S Chorghade1, Allison M Keys2

  • 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.

JACS Au
|August 30, 2024
PubMed
Summary
This summary is machine-generated.

CH-π interactions involving tryptophan 181 are crucial for galectin-3

More Related Videos

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads
08:48

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads

Published on: December 9, 2020

2.2K
Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.2K

Related Experiment Videos

Last Updated: Jun 14, 2025

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

3.3K
Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads
08:48

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads

Published on: December 9, 2020

2.2K
Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.2K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Glycan-binding proteins (lectins) mediate diverse biological functions.
  • Understanding protein-glycan interactions is key to targeting lectins in disease.
  • Aromatic residues and CH-π interactions are implicated in lectin binding sites.

Purpose of the Study:

  • To investigate the role of CH-π interactions in human galectin-3's binding to glycans.
  • To assess the impact of disrupting CH-π interactions on galectin-3 function.

Main Methods:

  • Site-directed mutagenesis of galectin-3 at W181, H158, and E184.
  • Experimental assays for glycan binding (lactose, mucins), hemagglutination.
  • Computational modeling and molecular simulations.

Main Results:

  • Galectin-3 variants with altered W181 residues showed significantly reduced binding to lactose, mucins, and red blood cells.
  • Disruption of CH-π interactions was as detrimental as disrupting hydrogen bonds.
  • Mutants exhibited decreased binding orientation stability.

Conclusions:

  • CH-π interactions involving W181 are critical for galectin-3's high-affinity lactose binding.
  • These interactions, alongside hydrogen bonding, enhance binding and are essential for function.
  • Findings support the development of novel lectin inhibitors targeting CH-π interactions.