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Related Concept Videos

Selectins01:25

Selectins

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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,...
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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...
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Fibronectins Connect Cells with ECM01:25

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Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
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Cell Adhesion Molecules - Types and Functions01:20

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Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
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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...
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Ligand Binding and Linkage00:49

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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...
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F-type lectins: Structural and functional aspects, and potential biomedical applications.

Gerardo R Vasta1, Mario A Bianchet2

  • 1Department of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Baltimore, MD 21202, United States.

BBA Advances
|July 4, 2025
PubMed
Summary
This summary is machine-generated.

F-type lectins (FTLs) are a newly identified group of fucose-binding proteins. Their diverse structures and broad distribution suggest significant roles in immunity, cell interactions, and potential applications in medicine.

Keywords:
DiagnosticEelFucolectinFucose lectin familyGlycan recognitionInnate immunityTherapeutic

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • F-type lectins (FTLs) represent a recently identified lectin family characterized by a distinct FTL domain (FTLD).
  • The FTL from the European eel (Anguilla anguilla) revealed a novel jellyroll lectin fold with unique fucose- and calcium-binding motifs.

Purpose of the Study:

  • To describe the structural and functional characteristics of F-type lectins.
  • To explore the diversity, distribution, and biological roles of FTLs.
  • To highlight potential applications of FTLs in medicine and biotechnology.

Main Methods:

  • Structural characterization of FTL from Anguilla anguilla.
  • Bioinformatic analysis of FTLD distribution and sequence motifs.
  • Review of FTL biological functions and potential applications.

Main Results:

  • FTLs possess a novel "F-type" fold with specific binding sites for fucose and calcium.
  • FTLs can exist as single or multiple domains, form oligomers, and exhibit diverse carbohydrate specificities.
  • FTLDs are widely distributed across various taxa but absent in placental mammals, suggesting evolutionary diversification.
  • FTLs are involved in innate immunity, fertilization, cell adhesion, and bacterial virulence.

Conclusions:

  • FTLs exhibit significant structural and functional diversity, with broad taxonomic distribution and varied biological roles.
  • The unique properties of FTLs offer promising avenues for applications in glycan analysis, cell separation, diagnostics, and therapeutics, particularly in cancer and infectious diseases.