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

The Nucleosome Core Particle02:10

The Nucleosome Core Particle

14.6K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
14.6K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.5K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
2.5K
Protein Complex Assembly02:41

Protein Complex Assembly

16.9K
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...
16.9K
Polymer Classification: Architecture01:14

Polymer Classification: Architecture

3.9K
Polymers are classified as linear or branched on the basis of their chain architecture. The polymer chains in linear polymers have a long chain-like structure with minimal to no branching at all. Even if a polymer features large substituent groups on the monomer, which appear as branches to the skeleton, it is not considered a branched polymer. A branched polymer contains secondary polymer chains that arise from the main polymer chain. The branching occurs when the polymer growth shifts from...
3.9K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.0K
Complex Numbers01:29

Complex Numbers

344
The real number system cannot represent the square root of a negative number, which restricts solutions for certain equations, such as quadratics with negative discriminants. To address this, the complex number system was developed, introducing the imaginary unit i, where i = √(-1). This extension allows for the representation of all roots, including those involving negative radicands.A complex number is written in the form x + yi, where x and y are real numbers. Here, x represents the...
344

You might also read

Related Articles

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

Sort by
Same author

Structural basis of cotranslational protein N-terminal acetylation by NatB in human cells.

Nature communications·2026
Same author

mTOR Substrate Phosphorylation in Growth Control: An Update.

Cancers·2026
Same author

Response to: Five methodological considerations for validating LLMs in risk of bias assessment.

Research synthesis methods·2026
Same author

Multi-omics profiling reveals divergent biology and liver microenvironment in HCC of metastatic and de novo origin.

Molecular cancer·2026
Same author

Exploring the potential of Claude 2 for risk of bias assessment: Using a large language model to assess randomized controlled trials with RoB 2.

Research synthesis methods·2026
Same author

Acid Versus Amide-Facts and Fallacies: A Case Study in Glycomimetic Ligand Design.

Molecules (Basel, Switzerland)·2025

Related Experiment Video

Updated: Feb 14, 2026

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
07:59

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination

Published on: August 17, 2022

2.3K

Architecture of the human mTORC2 core complex.

Edward Stuttfeld1, Christopher Hs Aylett2, Stefan Imseng1

  • 1Biozentrum, University of Basel, Basel, Switzerland.

Elife
|February 10, 2018
PubMed
Summary

Researchers revealed the structure of the mammalian target of rapamycin complex 2 (mTORC2), a key regulator of cell growth. This finding uncovers a protein binding site and explains why mTORC2 is insensitive to rapamycin.

Keywords:
cell growthelectron microscopyhumanmolecular biophysicsregulationstructural biology

More Related Videos

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

15.0K
Microfluidic Fabrication of Core-Shell Microcapsules carrying Human Pluripotent Stem Cell Spheroids
10:51

Microfluidic Fabrication of Core-Shell Microcapsules carrying Human Pluripotent Stem Cell Spheroids

Published on: October 13, 2021

3.7K

Related Experiment Videos

Last Updated: Feb 14, 2026

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
07:59

Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination

Published on: August 17, 2022

2.3K
Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

15.0K
Microfluidic Fabrication of Core-Shell Microcapsules carrying Human Pluripotent Stem Cell Spheroids
10:51

Microfluidic Fabrication of Core-Shell Microcapsules carrying Human Pluripotent Stem Cell Spheroids

Published on: October 13, 2021

3.7K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • The mammalian target of rapamycin (mTOR) is a crucial protein kinase regulating cellular metabolism and growth.
  • mTOR functions within two distinct complexes, mTORC1 and mTORC2.
  • Aberrant mTOR signaling is implicated in diseases such as cancer, diabetes, and neurological disorders.

Purpose of the Study:

  • To determine the architecture of the human mTORC2 complex.
  • To identify structural features of mTORC2, including accessory protein binding sites.
  • To elucidate the structural basis for mTORC2's insensitivity to rapamycin.

Main Methods:

  • Intermediate-resolution structural analysis of human mTORC2.
  • Biochemical and biophysical techniques to characterize the complex and its interactions.

Main Results:

  • The study reports the intermediate-resolution architecture of human mTORC2.
  • A conserved binding site for accessory proteins on mTOR within the complex was identified.
  • The structural findings provide an explanation for the rapamycin insensitivity of mTORC2.

Conclusions:

  • The determined architecture of mTORC2 offers insights into its regulation and function.
  • Understanding the structural basis of mTORC2's rapamycin insensitivity is critical for therapeutic development.
  • This work lays the foundation for further structural and functional studies of mTORC2 in health and disease.