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

Metal ion binding and conformational transitions in concanavalin A: a structure-function study.

C F Brewer1, R D Brown, S H Koenig

  • 1Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461.

Journal of Biomolecular Structure & Dynamics
|December 1, 1983
PubMed
Summary
This summary is machine-generated.

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

Nerve block efficacy in breast augmentation: A systematic review and meta-analysis.

Journal of plastic, reconstructive & aesthetic surgery : JPRAS·2023
Same author

Platelet-Rich Plasma (PRP) for Sacrococcygeal Pilonidal Disease: An Updated Systematic Review and Meta-Analysis.

World journal of surgery·2022
Same author

Chyle leak following total colectomy for ulcerative colitis: a case report and review of the literature.

Annals of the Royal College of Surgeons of England·2021
Same author

Purple Urine Bag Syndrome in a Patient with an Ileal Conduit and Clostridium Difficile Infection.

Acute medicine·2020
Same author

Phosphorylated human lectin galectin-3: analysis of ligand binding by histochemical monitoring of normal/malignant squamous epithelia and by isothermal titration calorimetry.

Anatomia, histologia, embryologia·2008
Same author

Lectin cross-linking interactions with multivalent carbohydrates.

Advances in experimental medicine and biology·2003

Concanavalin A (Con A) exhibits two forms: unlocked (weak binding) and locked (strong binding), with metal ions like Mn2+ and Ca2+ stabilizing the locked, active state. This conformational change is key to its saccharide binding activity.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Conformation

Background:

  • Concanavalin A (Con A) lectin's affinity for saccharides and requirement for metal ions (Mn2+, Ca2+) are well-established.
  • The detailed relationship between metal ion binding and saccharide binding activity in Con A has been a recent focus.
  • Con A exists in two conformational states: 'locked' (high affinity) and 'unlocked' (low affinity).

Purpose of the Study:

  • To explore the relationship between metal ion binding and conformational transitions in Con A.
  • To understand how these transitions determine the lectin's saccharide binding activity.

Main Methods:

  • Kinetic analysis of the transition from unlocked to locked Con A conformations.
  • Investigation of metal ion (Mn2+, Ca2+) binding effects on Con A conformation and activity.

Related Experiment Videos

  • X-ray crystallography to elucidate structural changes during conformational transitions.
  • Main Results:

    • The unlocked form, predominant in demetallized apo-Con A, weakly binds metal ions and saccharides.
    • The locked form binds metal ions, exhibiting full saccharide binding activity.
    • The transition involves cis-trans isomerization of an Ala-Asp peptide bond, with slow interconversions (minutes to days) due to high activation energy.

    Conclusions:

    • Metal ion binding stabilizes the locked conformation of Con A, enhancing saccharide affinity.
    • The slow conformational transition kinetics allow for the formation of various metastable Con A complexes.
    • Characterization of binary, ternary, and quaternary complexes provides insights into metal ion and saccharide binding dynamics.