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

The black widow's versatile venom.

H R Saibil

    Nature Structural Biology
    |January 14, 2000
    PubMed
    Summary
    This summary is machine-generated.

    The structure of tetrameric alpha-latrotoxin was revealed using cryo-electron microscopy. This spider neurotoxin features a pore complex with arms potentially binding receptors for synaptic vesicle release.

    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

    Structural analysis of macromolecular assemblies by electron microscopy.

    Chemical reviews·2011
    Same author

    Chaperonin complex with a newly folded protein encapsulated in the folding chamber.

    Nature·2009
    Same author

    Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding.

    Advances in protein chemistry·2002
    Same author

    Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane.

    Journal of molecular biology·2002
    Same author

    ATP-bound states of GroEL captured by cryo-electron microscopy.

    Cell·2002
    Same author

    Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy.

    Journal of structural biology·2001
    Same journal

    Fingering nucleic acids: the RNA did it.

    Nature structural biology·2003
    Same journal

    Histone H1.2 as a trigger for apoptosis.

    Nature structural biology·2003
    Same journal

    Tom40: more than just a channel.

    Nature structural biology·2003
    Same journal

    Announcing the worldwide Protein Data Bank.

    Nature structural biology·2003
    Same journal

    Small RNAs come of age.

    Nature structural biology·2003
    Same journal

    Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.

    Nature structural biology·2003
    See all related articles

    Area of Science:

    • Structural biology
    • Neuroscience
    • Biochemistry

    Background:

    • Alpha-latrotoxin is a potent spider neurotoxin.
    • Synaptic vesicle exocytosis is crucial for neurotransmission.

    Discussion:

    • Single particle cryo-electron microscopy (cryo-EM) was employed to determine the structure.
    • The tetrameric structure reveals a distinct pore complex.
    • Extended arms on the toxin may mediate receptor binding.

    Key Insights:

    • The high-resolution structure of tetrameric alpha-latrotoxin has been elucidated.
    • A pore complex with potential receptor-binding domains was identified.
    • This provides a structural basis for the toxin's mechanism of action.

    Outlook:

    Related Experiment Videos

    • Further studies can explore the precise interaction of the arms with synaptic receptors.
    • Understanding this interaction could lead to new therapeutic strategies for neurological disorders.
    • The structural data can guide the design of toxin analogs or inhibitors.