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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

Alkali Metals

Alkali Metals

Group 1 elements are soft and shiny metallic solids. They are malleable, ductile, and good conductors of heat and electricity. The melting points of the alkali metals are unusually low for metals and decrease going down the group, while the density increases going down the group with the exception of potassium (Table 1).
Table 1: Properties of the alkali metals

Ligand-gated Ion Channels

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...

Ligand-gated Ion Channels

Ligand-gated Ion Channels

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...

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Related Experiment Video

Updated: Apr 18, 2026

A Protocol for Safe Lithiation Reactions Using Organolithium Reagents

A Protocol for Safe Lithiation Reactions Using Organolithium Reagents

Published on: November 12, 2016

A ligand for ALK.

Greg Lemke¹, Erin D Lew²

¹Molecular Neurobiology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA. lemke@salk.edu.

Science Signaling

|January 22, 2015

Summary

This summary is machine-generated.

Researchers identified heparin as the elusive ligand that binds to and activates anaplastic lymphoma kinase (ALK). This discovery sheds light on ALK

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Last Updated: Apr 18, 2026

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Published on: November 12, 2016

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Area of Science:

Biochemistry
Molecular Biology
Oncology

Background:

Anaplastic lymphoma kinase (ALK) is a receptor tyrosine kinase implicated in various cancers due to aberrant activation, mutation, or overexpression.
The endogenous ligand responsible for normal ALK activation in vertebrates has remained unidentified, hindering a complete understanding of ALK signaling pathways.

Purpose of the Study:

To identify the endogenous ligand that binds to and activates anaplastic lymphoma kinase (ALK) in vertebrates.

Main Methods:

The study involved biochemical assays to test potential interactions between ALK and various molecules.
Specific experiments were designed to confirm the binding and activation of ALK by the identified ligand.

Main Results:

Heparin was identified as the molecule that binds to anaplastic lymphoma kinase (ALK).
The binding of heparin to ALK leads to the activation of the kinase.

Conclusions:

Heparin is the previously elusive ligand for anaplastic lymphoma kinase (ALK).
This finding provides crucial insights into the physiological regulation of ALK and has implications for cancer research.