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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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,...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

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Related Experiment Video

Updated: Jul 4, 2026

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
10:27

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

Published on: December 5, 2019

RING domains functioning as E3 ligases reveal distinct structural features: a molecular dynamics simulation study.

J-H Zhao1, C-T Yang, J W Wu

  • 1Department of Chemical Engineering and Biotechnology, National Taipei University of Technology, 1 Sec. 3 ZhongXiao E. Rd., Taipei 10608, Taiwan.

Journal of Biomolecular Structure & Dynamics
|June 7, 2008
PubMed
Summary
This summary is machine-generated.

The RING domain

Related Experiment Videos

Last Updated: Jul 4, 2026

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
10:27

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

Published on: December 5, 2019

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Dynamics

Background:

  • RING domains are cysteine-rich motifs crucial for biological processes.
  • They play a key role in the ubiquitinylation pathway as E3 ligases.
  • Understanding their structural features is vital for elucidating their function.

Purpose of the Study:

  • To investigate the distinct structural features of RING domains with E3 ligase function.
  • To compare the structural stability of RING domains with and without E3 ligase activity.
  • To identify key structural determinants for E3 ligase function in RING domains.

Main Methods:

  • Conducted molecular dynamics simulations.
  • Analyzed structural stability of recognition sites.
  • Examined distances between recognition and zinc ion binding sites.
  • Assessed secondary and tertiary structural stability.

Main Results:

  • Structural stability of the recognition site is essential for E3 ligase function.
  • Hydrophobic core and hydrogen bonding network maintain recognition site stability.
  • Stable distances between recognition and zinc ion binding sites are critical.
  • RING domains with E3 ligase function show lower beta stability due to proline residues.

Conclusions:

  • Structural stability of the recognition site and zinc ion binding sites are key for RING domain E3 ligase activity.
  • Lower beta stability in E3 ligase RING domains is linked to proline content.
  • These findings provide insights into the structure-function relationship of RING domains.