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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.8K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.0K
15.0K
Protein Complex Assembly02:41

Protein Complex Assembly

16.7K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.7K
Molecular Shape and Polarity03:37

Molecular Shape and Polarity

75.4K
Dipole Moment of a Molecule
75.4K
What is the Immune System?01:38

What is the Immune System?

127.6K
Overview
127.6K
Humoral Immune Responses01:36

Humoral Immune Responses

83.8K
Overview
83.8K

You might also read

Related Articles

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

Sort by
Same author

Phospholipid-driven conformational switching of HCV NS5A links protein folding to replication membrane remodeling.

Science advances·2026
Same author

Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.

Nature communications·2026
Same author

Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.

Journal of chemical theory and computation·2026
Same author

Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex.

Science advances·2026
Same author

Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules.

Cell reports·2025
Same author

Engineering Mesoscale T Cell Receptor Clustering by Plug-and-Play Nanotools.

Advanced materials (Deerfield Beach, Fla.)·2024

Related Experiment Video

Updated: Jan 29, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

3.2K

MHC I chaperone complexes shaping immunity.

Christoph Thomas1, Robert Tampé1

  • 1Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt/Main, Germany.

Current Opinion in Immunology
|February 17, 2019
PubMed
Summary
This summary is machine-generated.

Major histocompatibility complex class I (MHC I) molecules present peptides for immune detection. Structural studies reveal how peptide loading and editing by chaperones ensure stable, high-affinity peptide-MHC I complexes for T cell surveillance.

More Related Videos

Negative Additive Manufacturing of Complex Shaped Boron Carbides
06:45

Negative Additive Manufacturing of Complex Shaped Boron Carbides

Published on: September 18, 2018

9.1K
A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
07:59

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

15.6K

Related Experiment Videos

Last Updated: Jan 29, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

3.2K
Negative Additive Manufacturing of Complex Shaped Boron Carbides
06:45

Negative Additive Manufacturing of Complex Shaped Boron Carbides

Published on: September 18, 2018

9.1K
A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
07:59

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

15.6K

Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Cell Biology

Background:

  • Major histocompatibility complex class I (MHC I) molecules present endogenous peptides on cell surfaces, crucial for immune surveillance against infected or malignant cells.
  • Peptide loading onto MHC I involves the transporter associated with antigen processing (TAP) and ER-resident aminopeptidases (ERAP1/2) within the peptide-loading complex (PLC).
  • Peptide editing by chaperones like tapasin and TAPBPR ensures the selection of high-affinity peptides, stabilizing the peptide-MHC I (pMHC I) complex.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying MHC I peptide loading and proofreading.
  • To understand the dynamic interactions within the peptide-loading complex (PLC) and TAPBPR-MHC I complexes.
  • To highlight the conformational plasticity of proteins involved in MHC I peptide selection.

Main Methods:

  • Single-particle cryo-electron microscopy (cryo-EM)
  • X-ray crystallography
  • Nuclear Magnetic Resonance (NMR) spectroscopy

Main Results:

  • Recent structural studies have provided fundamental insights into the mechanisms of MHC I peptide loading and proofreading.
  • The dynamic nature of the PLC and TAPBPR-MHC I complexes has been highlighted.
  • The conformational plasticity of individual proteins involved in peptide selection is crucial for stable pMHC I complex formation.

Conclusions:

  • Structural insights reveal the intricate processes of peptide selection and stabilization for MHC I presentation.
  • Understanding these mechanisms is key to comprehending T cell recognition and immune responses.
  • The dynamic and plastic nature of the involved protein complexes facilitates efficient and accurate peptide loading onto MHC I molecules.