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Selectins

Selectins

Cell adhesion is an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

Types of Signaling Molecules

Types of Signaling Molecules

In multicellular organisms, many molecules transmit signals between cells to pass information. These signals vary in complexity and include small peptides, nucleotides, steroids, fatty acid derivatives, and dissolved gases such as nitric oxide. Some signaling molecules diffuse through the plasma membrane to act locally between neighboring cells or travel long distances. Others remain attached to the cell surface, transmitting information to other cells only when they make contact. In some...

Types of Signaling Molecules

Types of Signaling Molecules

In multicellular organisms, many molecules transmit signals between cells to pass information. These signals vary in complexity and include small peptides, nucleotides, steroids, fatty acid derivatives, and dissolved gases such as nitric oxide. Some signaling molecules diffuse through the plasma membrane to act locally between neighboring cells or travel long distances. Others remain attached to the cell surface, transmitting information to other cells only when they make contact. In some...

Assembly of Signaling Complexes

Assembly of Signaling Complexes

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,...

Metal-Ligand Bonds

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...

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Updated: Jun 9, 2026

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

Multivalent ligands for siglecs.

Mary K O'Reilly¹, James C Paulson

¹Department of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.

Methods in Enzymology

|September 7, 2010

Summary

This summary is machine-generated.

Multivalent ligands are essential tools for studying Siglecs (sialic acid-binding immunoglobulin-like lectins), enabling researchers to probe their function on immune cells and in recombinant systems.

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Last Updated: Jun 9, 2026

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

A Protocol for the Production of KLRG1 Tetramer

A Protocol for the Production of KLRG1 Tetramer

Published on: January 12, 2010

Area of Science:

Immunology
Glycobiology
Molecular Biology

Background:

Siglecs are immunomodulatory glycan-binding proteins involved in cell-cell interactions.
Siglec expression varies across immune cells, necessitating specific tools for functional studies.
Binding of cis ligands complicates the study of Siglec-ligand interactions.

Purpose of the Study:

To describe the use of multivalent ligands for probing Siglec function.
To investigate Siglec-ligand interactions on native cell surfaces and with recombinant Siglecs.

Main Methods:

Design and synthesis of multivalent ligands.
Application of multivalent ligands to probe cell surfaces.
Utilizing multivalent ligands to study Siglec binding to recombinant proteins.

Main Results:

Multivalency is required to overcome cis-ligand competition for stable Siglec binding.
Multivalent ligands effectively probe Siglec function on various immune cells.
Ligand binding to recombinant Siglecs can be investigated using this approach.

Conclusions:

Multivalent ligands are powerful tools for understanding Siglec biology.
These ligands facilitate the study of Siglec-mediated cellular interactions.
The described methods advance research into Siglec function and therapeutic targeting.