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

Septins01:19

Septins

Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Tight Junctions01:29

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Protein Complex Assembly02:41

Protein Complex Assembly

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...

You might also read

Related Articles

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

Sort by
Same author

ESCRT-III assembles around mis-segregated DNA to protect genome stability.

Nature structural & molecular biology·2026
Same author

Phosphatidylinositol diphosphate binding by ESCRT-III filaments.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

A prevalent disease-associated SNP in the human <i>ID3</i> gene regulates E-protein activity and cellular proliferation.

NAR molecular medicine·2026
Same author

Lenacapavir allosterically remodels the HIV-1 capsid.

bioRxiv : the preprint server for biology·2026
Same author

RNA splicing is required for timely completion of abscission and is modulated by the abscission checkpoint.

bioRxiv : the preprint server for biology·2025
Same author

Mechanism of Phosphatidylserine Lipid Scrambling by Human SERINC3, an HIV-1 Restriction Factor.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Jun 5, 2026

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Hexagonal assembly of a restricting TRIM5alpha protein.

Barbie K Ganser-Pornillos1, Viswanathan Chandrasekaran, Owen Pornillos

  • 1Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.

Proceedings of the National Academy of Sciences of the United States of America
|December 29, 2010
PubMed
Summary

Tripartite motif-containing 5 alpha (TRIM5α) proteins restrict retroviral infections by forming hexagonal lattices that bind viral capsids. This assembly mechanism enhances TRIM5α’s ability to recognize and block a broad range of retroviruses.

More Related Videos

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Related Experiment Videos

Last Updated: Jun 5, 2026

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • TRIM5α proteins act as restriction factors against retroviral infections in mammalian cells.
  • They function by binding viral capsids, promoting dissociation, and inhibiting reverse transcription.
  • TRIM5α isoforms, like rhesus monkey TRIM5α and TRIM5-21R, exhibit broad retroviral recognition.

Purpose of the Study:

  • To investigate the self-assembly properties of the TRIM5-21R protein.
  • To elucidate the structural basis of TRIM5α's broad retroviral recognition mechanism.

Main Methods:

  • Recombinant TRIM5-21R protein expression and purification.
  • Analysis of protein self-assembly using electron microscopy.
  • Investigating the role of specific protein domains (SPRY, B-box 2) and dimerization in assembly.
  • Studying the effect of HIV-1 CA protein arrays on TRIM5-21R assembly.

Main Results:

  • Recombinant TRIM5-21R spontaneously forms two-dimensional hexagonal lattices.
  • Lattice formation requires protein dimerization and a specific B-box 2 residue (Arg121), but not the SPRY domain.
  • Assembly is promoted by binding to hexagonal arrays of HIV-1 CA protein, mimicking viral capsids.
  • TRIM5α assembly appears to be templated by the viral capsid surface symmetry.

Conclusions:

  • TRIM5α proteins utilize a templated self-assembly mechanism to restrict retroviruses.
  • The formation of deformable hexagonal scaffolds allows TRIM5α to adapt and bind diverse viral capsid symmetries.
  • This mechanism involves synergistic interactions including direct binding, avidity, and lattice complementarity for efficient capsid recognition.