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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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Complexation Equilibria: The Chelate Effect01:19

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In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
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Ligand Binding Sites02:40

Ligand Binding Sites

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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.
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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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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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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
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Activation of Integrins01:15

Activation of Integrins

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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Related Experiment Video

Updated: Apr 8, 2026

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium
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Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium

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E-selectin ligand complexes adopt an extended high-affinity conformation.

Roland C Preston1, Roman P Jakob2, Florian P C Binder1

  • 1Institute of Molecular Pharmacy, Universität Basel, 4056 Basel, Switzerland.

Journal of Molecular Cell Biology
|June 29, 2015
PubMed
Summary
This summary is machine-generated.

E-selectin

Keywords:
E-selectinconformational changeglycomimetic antagonistinflammationleukocyte adhesionsialyl Lewisx

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • E-selectin mediates leukocyte rolling in inflammation by binding sialyl Lewis(x) (sLe(x)).
  • Efficient leukocyte recruitment relies on catch-bond interactions under flow.
  • Understanding E-selectin's molecular mechanism is crucial for anti-inflammatory drug development.

Purpose of the Study:

  • To elucidate the structural basis of E-selectin's catch-bond behavior.
  • To reveal the molecular mechanism linking ligand binding to conformational changes.
  • To provide insights for designing novel selectin antagonists.

Main Methods:

  • X-ray crystallography to determine co-crystal structures.
  • Molecular dynamics simulations to analyze binding affinity and conformational states.
  • Small-angle X-ray scattering to study ligand-induced conformational transitions.

Main Results:

  • Identified an extended E-selectin conformation as a high-affinity binding state.
  • Demonstrated a direct link between sLe(x) binding and conformational changes in solution.
  • Revealed a series of structural changes underlying catch-bond-mediated leukocyte recruitment.

Conclusions:

  • Ligand binding induces conformational stretching in E-selectin, explaining catch-bond behavior.
  • The detailed molecular insights facilitate the design of new therapeutic selectin antagonists.
  • This research supports the development of drugs targeting inflammatory diseases.