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

Peptide binding by class I and class II MHC molecules

M A Batalia1, E J Collins

  • 1Department of Microbiology and Immunology, University of North Carolina at Chapel Hill 27599-7290, USA.

Biopolymers
|January 1, 1997
PubMed
Summary

Major histocompatibility complex (MHC) antigens bind diverse peptides for immune protection. Understanding these binding forces is crucial for developing peptide-based therapies, though predicting specific binding remains challenging.

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

Mutational analysis of hemoglobin binding and heme utilization by a bacterial hemoglobin receptor.

Journal of bacteriology·2013
Same author

Allelic diversity at the DLA-88 locus in Golden Retriever and Boxer breeds is limited.

Tissue antigens·2012
Same author

Should females prefer to mate with low-quality males?

Journal of theoretical biology·2008
Same author

Treatment-resistance to clozapine in association with ultrarapid CYP1A2 activity and the C-->A polymorphism in intron 1 of the CYP1A2 gene: effect of grapefruit juice and low-dose fluvoxamine.

Journal of clinical psychopharmacology·2002
Same author

Enhancing cytotoxic T cell responses with altered-peptide ligands.

Archivum immunologiae et therapiae experimentalis·2001
Same author

T cell activity correlates with oligomeric peptide-major histocompatibility complex binding on T cell surface.

The Journal of biological chemistry·2001

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Major histocompatibility complex (MHC) antigens are crucial for adaptive immunity, presenting peptides to T cells.
  • MHC molecules bind a wide range of peptides to ensure comprehensive host defense against pathogens.
  • Dysregulation in peptide recognition by MHC molecules can lead to autoimmune diseases like rheumatoid arthritis.

Purpose of the Study:

  • To review current understanding of peptide binding mechanisms by MHC molecules.
  • To highlight the importance of peptide-MHC interactions for immunological protection and disease.
  • To assess the utility of crystallographic data in predicting high-affinity peptide binding to MHC.

Main Methods:

  • Summary of crystallographic analyses of peptide binding to class I and class II MHC molecules.

Related Experiment Videos

  • Review of existing literature on the forces governing peptide-MHC interactions.
  • Analysis of data to evaluate predictive capabilities for peptide binding affinity.

    • Main Results:

    • Crystallographic data have significantly advanced the understanding of how MHC molecules bind diverse peptides.
    • Despite progress, current data do not enable accurate prediction of which specific peptides will bind with high affinity to a given MHC molecule.
    • Insights into peptide binding forces are essential for advancing peptide-based immunotherapies.

    Conclusions:

    • Understanding peptide-MHC binding is critical for developing effective immunotherapies.
    • Further research is needed to improve the predictive power of peptide binding to MHC molecules.
    • Structural data provide valuable mechanistic insights but are insufficient for precise binding prediction.