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Related Concept Videos

Selectins01:25

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...
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...
Immunoglobulin-like Cell Adhesion Molecules01:31

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...
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...
Membrane Carbohydrates01:30

Membrane Carbohydrates

The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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.
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Bridging lectin binding sites by multivalent carbohydrates.

Valentin Wittmann1, Roland J Pieters

  • 1Department of Chemistry and Konstanz Research School Chemical Biology, University of Konstanz, Universitätsstr. 10, 78457 Konstanz, Germany. mail@valentin-wittmann.de

Chemical Society Reviews
|April 20, 2013
PubMed
Summary

Multivalency enhances carbohydrate-protein interactions through chelation, where ligands bind multiple sites on receptors. This review covers various chelating lectin ligands, highlighting their biological significance.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Carbohydrate-protein interactions are crucial for biological recognition.
  • Weak individual interactions necessitate multivalency for significant binding affinity and selectivity.
  • Chelation, a form of multivalency, significantly enhances binding by engaging multiple receptor sites.

Purpose of the Study:

  • To review recent examples of chelating lectin ligands.
  • To discuss the impact of ligand size and receptor binding site distance on chelation.
  • To highlight the importance of experimental validation for chelating binding.

Main Methods:

  • Literature review of studies on carbohydrate-protein interactions and multivalency.
  • Analysis of reported distances between binding sites on various lectins.
  • Summary of known chelating lectin ligands and their properties.

Main Results:

  • Examples of chelating lectin ligands for diverse lectins are presented, including toxins and antibodies.
  • The shortest distances between binding sites range from ~9 Å (Shiga-like toxin) to 100 Å (RCA120, ECL).
  • Chelating binding is inferred for most discussed ligands, but experimental proof (e.g., X-ray crystallography) is limited.

Conclusions:

  • Chelation is a key mechanism for achieving high-affinity carbohydrate-protein interactions.
  • A variety of lectins can engage in chelating binding with multivalent ligands.
  • Further experimental studies are needed to confirm chelating binding in many cases.