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

Structural Organization of the Human Body: An Overview01:18

Structural Organization of the Human Body: An Overview

30.1K
It is convenient to consider the body's structures in terms of fundamental levels of organization that increase in complexity: subatomic particles, atoms, molecules, organelles, cells, tissues, organs, organ systems, and organisms.
To study the chemical level of organization, scientists consider the simplest building blocks of matter: subatomic particles, atoms, and molecules. All matter in the universe is composed of one or more unique pure substances called elements, familiar examples of...
30.1K
Structures of Solids02:22

Structures of Solids

18.6K
Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
18.6K
Structural Isomerism02:34

Structural Isomerism

21.8K
Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
Linkage isomers occur when the coordination compound contains a ligand that can bind to the transition metal center through two different atoms. For example, the CN− ligand can bind through the carbon atom or through the nitrogen atom. Similarly, SCN− can...
21.8K
Chromosome Structure02:40

Chromosome Structure

26.7K
A functional eukaryotic chromosome must contain three elements: a centromere, telomeres, and numerous origins of replication.
The centromere is a DNA sequence that links sister chromatids. This is also where kinetochores, protein complexes to which spindle microtubules attach, are constructed after the chromosome is replicated. The kinetochores allow the spindle microtubules to move the chromosomes within the cell during cell division.
Telomeres consist of non-coding repetitive nucleotide...
26.7K
Structure of Lipids03:38

Structure of Lipids

99.4K
Lipids include a diverse group of compounds that are largely nonpolar in nature. This is because they are hydrocarbons that include mostly nonpolar carbon-carbon or carbon-hydrogen bonds. Non-polar molecules are hydrophobic (“water fearing”), or insoluble in water. Lipids perform many different functions in a cell. Cells store energy for long-term use in the form of fats. Lipids also provide insulation from the environment for plants and animals. For example, they help keep aquatic...
99.4K
Viral Structure00:56

Viral Structure

74.8K
Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
74.8K

You might also read

Related Articles

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

Sort by
Same author

Phenotypic CRISPR screens identify NLRX1 as an essential activator of the human mitochondrial permeability transition.

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

Allosteric coupling between PIP<sub>2</sub> and Ca<sup>2+</sup> binding sites gates TMEM16A channels.

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

A Multimodal Adaptive Optical Microscope For <i>In Vivo</i> Imaging from Molecules to Organisms.

bioRxiv : the preprint server for biology·2025
Same author

The SARS-CoV-2 accessory protein Orf3a is not an ion channel, but does interact with trafficking proteins.

eLife·2023
Same author

The SARS-CoV-2 accessory protein Orf3a is not an ion channel, but does interact with trafficking proteins.

bioRxiv : the preprint server for biology·2022
Same author

Visualizing synaptic dopamine efflux with a 2D composite nanofilm.

eLife·2022

Related Experiment Video

Updated: Feb 14, 2026

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

10.0K

Structure of full-length human TRPM4.

Jingjing Duan1, Zongli Li2,3, Jian Li4,5

  • 1Howard Hughes Medical Institute, Ashburn, VA 20147.

Proceedings of the National Academy of Sciences of the United States of America
|February 22, 2018
PubMed
Summary

The first electron cryomicroscopy structure of human TRPM4 (hTRPM4) reveals its closed state, identifying key gating mechanisms and regulatory interactions crucial for understanding heart block. This provides insights into TRPM4 channel function.

Keywords:
cardiac arrhythmiacryomicroscopyion channeltransient receptor potential channel

More Related Videos

Modeling Human Cerebellar Development In Vitro in 2D Structure
06:14

Modeling Human Cerebellar Development In Vitro in 2D Structure

Published on: September 16, 2022

2.1K
High-resolution Structural Magnetic Resonance Imaging of the Human Subcortex In Vivo and Postmortem
08:16

High-resolution Structural Magnetic Resonance Imaging of the Human Subcortex In Vivo and Postmortem

Published on: December 30, 2015

15.8K

Related Experiment Videos

Last Updated: Feb 14, 2026

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

10.0K
Modeling Human Cerebellar Development In Vitro in 2D Structure
06:14

Modeling Human Cerebellar Development In Vitro in 2D Structure

Published on: September 16, 2022

2.1K
High-resolution Structural Magnetic Resonance Imaging of the Human Subcortex In Vivo and Postmortem
08:16

High-resolution Structural Magnetic Resonance Imaging of the Human Subcortex In Vivo and Postmortem

Published on: December 30, 2015

15.8K

Area of Science:

  • Structural biology
  • Ion channel biophysics
  • Cardiovascular research

Background:

  • Transient receptor potential melastatin subfamily member 4 (TRPM4) is a calcium-activated, monovalent-selective cation channel.
  • Mutations in human TRPM4 (hTRPM4) are linked to progressive familial heart block, highlighting its critical role in cardiac function.

Purpose of the Study:

  • To determine the high-resolution structure of human TRPM4 in a closed state.
  • To elucidate the gating mechanisms and regulatory interactions of hTRPM4.

Main Methods:

  • Electron cryomicroscopy (cryo-EM) was used to resolve the structure of hTRPM4.
  • The structure was determined at a resolution of 3.7 Å in a closed, Na+-bound, apo state at pH 7.5.

Main Results:

  • The structure reveals an upper gate in the selectivity filter and a lower gate at the cytoplasmic coiled-coil domain entrance.
  • Five sodium ions are localized within the pore and at the coiled-coil domain entrance.
  • Identified intramolecular interactions, aromatic interactions (π-π, cation-π), extracellular glycosylation, a pore-loop disulfide bond, and lipid binding sites.

Conclusions:

  • The determined hTRPM4 structure provides a molecular basis for understanding its gating and regulation.
  • Insights into TRPM4 structure can inform the study of channelopathies like familial heart block.
  • This work offers a foundation for future investigations into TRPM4 function and modulation.