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Related Concept Videos

Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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...
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...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
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...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
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Related Experiment Video

Updated: Jun 15, 2026

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis
07:48

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis

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The adenovirus type 3 dodecahedron's RGD loop comprises an HSPG binding site that influences integrin binding.

E Gout1, G Schoehn, D Fenel

  • 1CNRS-Institut de Biologie Structurale, 41 rue Jules Horowitz, 38027 Grenoble, France.

Journal of Biomedicine & Biotechnology
|March 13, 2010
PubMed
Summary

Human adenovirus type 3 uses heparan sulfate proteoglycans (HSPGs) and integrins for cell entry. A downstream basic sequence is crucial for integrin docking, revealing a key interplay between these receptors.

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Last Updated: Jun 15, 2026

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis
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Published on: January 7, 2019

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Human adenovirus type 3 (HAdV3) pseudoparticles are versatile vectors for DNA and protein delivery.
  • Cellular entry involves interactions with Heparan Sulphate Proteoglycans (HSPGs) and integrins.

Purpose of the Study:

  • To elucidate the roles of the RGD loop and a downstream basic sequence in HAdV3 pseudoparticle cell entry.
  • To investigate the interplay between HSPGs and integrin receptors during viral attachment.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) reconstruction of HAdV3 pseudoparticles complexed with Heparan Sulphate (HS) oligosaccharides.
  • Site-directed mutagenesis to create RGE and basic sequence mutants (KQKR to AQAS).
  • Cell binding assays using HS-deficient cells (CHO-2241).

Main Results:

  • Mutation of the RGD sequence (RGE mutant) abolished binding to HS-deficient cells.
  • Mutation of the downstream basic sequence significantly reduced integrin recognition.
  • Cryo-EM revealed an extradensity on the RGD loop upon HS binding.

Conclusions:

  • The RGD sequence is essential for HSPG interaction.
  • A downstream basic sequence plays a critical role in integrin docking.
  • HSPGs and integrins exhibit a coordinated mechanism for HAdV3 cell entry.