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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.4K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.4K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.5K
2.5K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.8K
2.8K
Protein Folding01:22

Protein Folding

124.5K
Overview
124.5K
Protein Folding01:25

Protein Folding

10.0K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
10.0K
Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

17.0K
The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this...
17.0K

You might also read

Related Articles

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

Sort by
Same author

Encapsulation of apigenin into β-cyclodextrin metal-organic frameworks with high embedment efficiency and stability.

Food chemistry·2024
Same author

Research progress on plant-based protein Pickering particles: Stabilization mechanisms, preparation methods, and application prospects in the food industry.

Food chemistry: X·2024
Same author

Direct 4D printing of ceramics driven by hydrogel dehydration.

Nature communications·2024
Same author

Improved capacitive energy storage performance in hybrid films with ultralow aminated molybdenum trioxide integration for high-temperature applications.

Materials horizons·2024
Same author

Efficacy and safety of Lianhua Qingwen as an adjuvant treatment for influenza in Chinese patients: A meta-analysis.

Medicine·2024
Same author

Correlation of 20 Single-Nucleotide Polymorphisms with Weight and Wool Traits in Alpine Merino Sheep.

Animals : an open access journal from MDPI·2024

Related Experiment Video

Updated: Nov 17, 2025

Interactive Molecular Model Assembly with 3D Printing
06:15

Interactive Molecular Model Assembly with 3D Printing

Published on: August 13, 2020

10.6K

Mediator structure and conformation change.

Heqiao Zhang1, Dong-Hua Chen2, Rayees U H Mattoo2

  • 1Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 201210 Shanghai, China; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.

Molecular Cell
|February 11, 2021
PubMed
Summary
This summary is machine-generated.

Mediator, a key transcription adaptor, was structurally analyzed using cryo-EM. This revealed its near-atomic structure, including activator-binding sites, and how it changes upon RNA polymerase II interaction.

Keywords:
Mediatoractivatorconformation changecryo-EMpol IIstructuretranscription

More Related Videos

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

6.6K
Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

12.9K

Related Experiment Videos

Last Updated: Nov 17, 2025

Interactive Molecular Model Assembly with 3D Printing
06:15

Interactive Molecular Model Assembly with 3D Printing

Published on: August 13, 2020

10.6K
Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

6.6K
Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

12.9K

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Mediator is a crucial protein complex that bridges gene-specific transcription factors and the core RNA polymerase II (pol II) machinery.
  • Previous structural insights into Mediator were limited, lacking detail on activator-binding regions.

Purpose of the Study:

  • To determine the near-atomic resolution cryo-electron microscopy (cryo-EM) structure of the Mediator complex.
  • To visualize the Mediator's architecture, including activator and pol II interaction sites.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to resolve the Mediator complex structure at near-atomic resolution.

Main Results:

  • The cryo-EM structure revealed nearly all ordered amino acid residues of the Mediator complex.
  • Key activator-binding regions, including the Tail module and the Med1 subunit, were visualized.
  • Conformational changes were observed across the Mediator upon binding with RNA polymerase II, linking activator and pol II interfaces.

Conclusions:

  • The high-resolution structure provides unprecedented detail of the Mediator complex.
  • Understanding Mediator's structural dynamics in response to pol II is vital for deciphering transcription regulation.