Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Desmosomes01:05

Desmosomes

The term desmosome derives from the Greek words "desmo" and "soma" meaning "adhesion bodies." This structure was first observed during the late 1800s and described as small, dense nodules in the epidermis. Desmosomes are button-like structures that help form an interlinked network of intermediate filaments across the cells. These junctions are  essential to hold cells together under mechanical stress and to maintain tissue integrity. Desmosomes are multi-protein complexes comprising desmosomal...
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,...
Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Comparison of Child-Pugh and MELD scores in predicting survival of hepatocellular carcinoma patients with splenomegaly undergoing TACE: a real-world study.

Frontiers in medicine·2026
Same author

MTA-Swin: A Multi-Token Attention Swin Transformer for Brain Tumor Classification with Leakage-Free MRI Benchmarking.

Journal of medical systems·2026
Same author

Effects of Immunonutrition on Intestinal Microecology in Patients With Gastrointestinal Cancers: Mechanisms and Clinical Applications.

Nutrition reviews·2026
Same author

Synthesis of 3-Difluoromethyl-1,3,4-oxadiazole-thiones from Aroylhydrazides, TMSCF<sub>3</sub>, and Elemental Sulfur.

The Journal of organic chemistry·2026
Same author

From technology to interaction: How ritual interaction drives participation intention in immersive digital environments.

iScience·2026
Same author

Time-course of post-activation performance enhancement (PAPE) following multi-dimensional elastic band vs. heavy resistance exercise.

Frontiers in physiology·2026
Same journal

Chemical, Biological, and Ecological Evidence for Aerobic Deoxynivalenol Detoxification in Agronomic Soil-Derived Bacterial Communities.

Toxins·2026
Same journal

Botulinum Toxin Treatment for Uncommon Phenotypes of Laryngeal Adductor Breathing Dystonia.

Toxins·2026
Same journal

Enhancing Neuronal Networks with <i>Rhinella schneideri</i> Skin Secretion Molecules: Implications for Neurodegenerative Disorders.

Toxins·2026
Same journal

Dangerous Measures: A Case Report and Review of Motoro Ray Envenomation.

Toxins·2026
Same journal

The Impact of OnabotulinumtoxinA on Oral Pain Medication Prescription Fills and Low-Value Care in Patients with Cervical Dystonia in the United States: A Retrospective Claims Analysis.

Toxins·2026
Same journal

Broad-Spectrum Antiviral and Antibacterial Activity of the Scorpion Venom Peptide HP1090.

Toxins·2026
See all related articles

Related Experiment Video

Updated: May 27, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

ADAM-15 disintegrin-like domain structure and function.

Dong Lu1, Mike Scully, Vijay Kakkar

  • 1Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK. xlu@tri-london.ac.uk

Toxins
|November 10, 2011
PubMed
Summary
This summary is machine-generated.

Human ADAM-15 is unique among ADAM proteins for its RGD motif, crucial for binding integrin receptors. This review explores RGD-containing domains and their role in antagonizing integrin function.

Keywords:
ADAM proteinRGD-motifSnake venom toxindisintegrinintegrin

More Related Videos

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

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex
07:17

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex

Published on: August 2, 2021

Related Experiment Videos

Last Updated: May 27, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

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

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex
07:17

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex

Published on: August 2, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • ADAM proteins are transmembrane cell-surface proteins involved in adhesion and proteolysis.
  • Human ADAM-15 uniquely possesses an Arg-Gly-Asp (RGD) motif in its disintegrin-like domain, a feature common in snake venom disintegrins.
  • This RGD motif is critical for binding integrin receptors.

Purpose of the Study:

  • To review the structural characteristics of RGD-containing disintegrin-like domains.
  • To elucidate the structural features enabling antagonism of integrin function.
  • To compare these structures to the canonical RGD template.

Main Methods:

  • Structural analysis of RGD-containing disintegrin-like domains.
  • Comparison of ADAM-15 RGD motif with other disintegrins.
  • Review of literature on integrin-disintegrin interactions.

Main Results:

  • The RGD motif in ADAM-15 acts as a specific integrin ligand binding site.
  • Structural features of RGD domains dictate their antagonistic activity against integrins.
  • ADAM-15's RGD motif shares similarities with snake venom disintegrins.

Conclusions:

  • ADAM-15's RGD motif is a key mediator of integrin interactions.
  • Understanding these structures provides insights into integrin regulation.
  • This review highlights the significance of the RGD motif in ADAM-15's biological functions.