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 Experiment Videos

Structural characterization of the ADAM 16 disintegrin loop active site.

Jeffrey W Norris1, Melanie M Tomczak, Ann E Oliver

  • 1Center For Biostabilization, University of California, 1 Shields Avenue, Davis, California 95616, USA. jwnorris@ucdavis.edu

Biochemistry
|August 13, 2003
PubMed
Summary

The N-terminal sequence of ADAM 16’s disintegrin loop activates Xenopus eggs by triggering calcium release, independent of integrin binding. This structural insight reveals the active site mechanism for ADAM-mediated egg activation.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion.

The Journal of clinical investigation·2026
Same author

Is Deficiency in the Electrical Current of Injury a Barrier to Healing in Hard-to-Heal Wounds? A Systematic Review with Implications for the TIMERS Paradigm.

Advances in wound care·2025
Same author

First-in-Human Clinical Feasibility Study of Ablation of Benign Thyroid Nodules Using Nanosecond Pulsed Field Ablation.

Thyroid : official journal of the American Thyroid Association·2025
Same author

Identification of the role of SEL1L in platelet function through a multi-species genetic investigation.

bioRxiv : the preprint server for biology·2025
Same author

Nano-Pulse Stimulation Therapy Initiates Regulated Cell Death in Skin, Unlike Bovie Radiofrequency Ablation and Cryoablation.

Bioelectricity·2024
Same author

The CellFX Percutaneous Electrode System for Nanosecond Pulsed Field Ablation.

Bioelectricity·2024

Area of Science:

  • Developmental Biology
  • Molecular Biology
  • Cell Biology

Background:

  • ADAMs (a disintegrin and metalloproteinase domain) are crucial for cell adhesion, often binding integrins via a disintegrin loop.
  • Xenopus laevis sperm ADAM 16's disintegrin loop peptides induce egg activation, mimicking fertilization events like intracellular calcium rise.

Purpose of the Study:

  • To characterize the specific portion of the ADAM 16 disintegrin loop responsible for initiating Xenopus egg activation.
  • To elucidate the structural and functional mechanisms underlying ADAM-mediated egg activation.

Main Methods:

  • Synthesized and tested peptides representing different parts of the ADAM 16 disintegrin loop for egg-activating activity.
  • Assessed peptide effects on liposome permeability and fluidity to infer membrane interaction mechanisms.

Related Experiment Videos

  • Utilized infrared spectroscopy to determine the secondary structure of the active peptide.

    • Main Results:

    • A peptide from the N-terminal half of the disintegrin loop activated eggs similarly to the full-length peptide, despite lacking a canonical integrin-binding sequence.
    • Peptides did not affect liposome properties, suggesting receptor-mediated signaling rather than direct membrane disruption.
    • Infrared spectroscopy revealed a beta-turn structure in the N-terminal region, crucial for activity, as a non-turn peptide failed to activate eggs.

    Conclusions:

    • The N-terminal region of the ADAM 16 disintegrin loop, particularly its beta-turn structure, is critical for egg activation.
    • Egg activation by ADAM 16 peptides occurs via a receptor-mediated pathway, not through direct membrane interaction.
    • These findings offer the first structural insights into the active site of an ADAM disintegrin loop and its role in fertilization.