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

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.5K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.5K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

2.4K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
2.4K
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
Protein Complex Assembly02:41

Protein Complex Assembly

2.5K
2.5K
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

5.3K
The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles,...
5.3K
RNA Structure01:23

RNA Structure

78.8K
Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA): messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three RNA types consist of a...
78.8K

You might also read

Related Articles

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

Sort by
Same author

Whole genome sequencing-based multi-locus association mapping for kernel iron, zinc and protein content in groundnut.

Scientific reports·2026
Same author

Mapping Fusarium wilt and sterility mosaic disease resistance-associated genomic regions and haplotype variants in pigeonpea.

BMC plant biology·2026
Same author

Conservation of Bacterial Lipopolysaccharide Binding by SARS-CoV-2 Spike across Major Viral Variants.

Computational and structural biotechnology journal·2026
Same author

Multiscale Simulations and Cryo-Electron Microscopy Reveal the Transition Pathway of Dengue Virus-like Particle Nanoassembly.

ACS nano·2026
Same author

Targeting the epidermal growth factor receptor using IgM antibodies: toward next generation cancer immunotherapy.

Frontiers in immunology·2026
Same author

Cross-linking mass spectrometry and structural modeling identifies compact conformation of DENV NS2B cofactor region bound to NS3.

Structure (London, England : 1993)·2026

Related Experiment Video

Updated: Jan 20, 2026

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

11.5K

The structural basis for membrane assembly of immunoreceptor signalling complexes.

Namita Dube1,2, Jan K Marzinek3, Robert C Glen1,4

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.

Journal of Molecular Modeling
|August 29, 2019
PubMed
Summary

Immunoreceptor complexes, like the T cell receptor (TCR), assemble via transmembrane (TM) domains. Their stability and signaling are influenced by lipid environment and phosphorylation, impacting immune responses.

Keywords:
ITAM motifLipid bilayerMolecular dynamics (MD) simulationT cell receptor (TCR)Transmembrane domain

More Related Videos

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

30.6K
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.4K

Related Experiment Videos

Last Updated: Jan 20, 2026

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

11.5K
Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

30.6K
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.4K

Area of Science:

  • Molecular biology
  • Biophysics
  • Immunology

Background:

  • Immunoreceptors are transmembrane complexes crucial for cell signaling.
  • Their structure and function are influenced by the surrounding membrane environment.
  • Understanding these interactions is key to deciphering immune cell activation.

Purpose of the Study:

  • To investigate the molecular dynamics of immunoreceptor complexes, specifically the T cell receptor (TCR)/CD3 and DAP12/NKG2C complexes.
  • To explore how lipid composition and phosphorylation affect the stability and conformation of these complexes.
  • To elucidate the role of the microenvironment in regulating immunoreceptor signaling.

Main Methods:

  • Utilized over 15 microseconds of atomic-resolution molecular dynamics (MD) simulations.
  • Employed a novel alchemical approach to simulate cytoplasmic tails at varying lipid bilayer depths.
  • Simulated transmembrane (TM) domains in different oligomerization states.

Main Results:

  • Receptor conformation and ITAM exposure are sensitive to lipid species and phosphorylation.
  • Stable membrane insertion during early assembly is facilitated by the lipid/solvent interface and charged residue ionization.
  • The cytoplasmic CD3ε tail's conformation is modulated by lipid enrichment and phosphorylation.

Conclusions:

  • Immunoreceptor complex architecture and signal transduction are tightly regulated by their microenvironment.
  • Lipid-protein interactions and charge states play critical roles in receptor assembly and function.
  • This study provides atomic-level insights into the dynamic regulation of immune signaling complexes.