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

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

15.1K
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...
15.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.2K
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,...
7.2K
Cholinergic Receptors: Muscarinic01:25

Cholinergic Receptors: Muscarinic

6.2K
The pharmacological actions of acetylcholine are elicited via its binding to two families of cholinergic receptors or cholinoceptors, namely, muscarinic and nicotinic receptors. Muscarinic receptors are G protein-coupled receptors and have five subtypes, M1–M5. All mAChR subtypes are activated by acetylcholine and blocked by the antagonist, atropine. 
The subtypes M1, M3, and M5 couple with the Gq subunit and activate the phospholipase C (PLC) activity, mobilizing intracellular Ca2+....
6.2K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

20.0K
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
20.0K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

8.6K
G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
8.6K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.9K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.9K

You might also read

Related Articles

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

Sort by
Same author

CTCF directly binds G-quadruplex structures to regulate genome topology and gene expression.

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

Per-ARNT-Sim (PAS) Domains in Basic Helix-Loop-Helix (bHLH)-PAS Transcription Factors and Coactivators: Structures and Mechanisms.

Journal of molecular biology·2023
Same author

Histone acetylation and deacetylation - Mechanistic insights from structural biology.

Gene·2023
Same author

Prostaglandins as Candidate Ligands for a Per-ARNT-Sim (PAS) Domain of Steroid Receptor Coactivator 1 (SRC1).

bioRxiv : the preprint server for biology·2023
Same author

Cryo-EM structure of the Saccharomyces cerevisiae Rpd3L histone deacetylase complex.

Nature communications·2023
Same author

Endoscopic Midline and Paramedian Supracerebellar Infratentorial Approaches to Pineal Region Tumors: A Clinical Study and Approach Comparison.

World neurosurgery·2022

Related Experiment Video

Updated: Apr 12, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K

Structural Basis for Multi-specificity of MRG Domains.

Tao Xie1, Adam M Zmyslowski1, Yongbo Zhang2

  • 1Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.

Structure (London, England : 1993)
|May 12, 2015
PubMed
Summary

Chromatin protein MRGBP binds the MRG15 MRG domain using a similar mechanism to Pf1, despite lacking sequence similarity. This reveals how MRG domains evolve to interact with diverse protein targets.

More Related Videos

Screening Peptides that Activate MRGPRX2 using Engineered HEK Cells
12:38

Screening Peptides that Activate MRGPRX2 using Engineered HEK Cells

Published on: November 6, 2021

3.2K
Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

3.9K

Related Experiment Videos

Last Updated: Apr 12, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K
Screening Peptides that Activate MRGPRX2 using Engineered HEK Cells
12:38

Screening Peptides that Activate MRGPRX2 using Engineered HEK Cells

Published on: November 6, 2021

3.2K
Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

3.9K

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Protein Interactions

Background:

  • Chromatin-binding proteins are crucial for organizing protein complexes at specific genomic locations.
  • MRG15 is a key protein that recruits complexes involved in gene regulation, DNA repair, and RNA splicing.
  • Previous research identified interaction requirements between the MRG domain of MRG15 and its partner Pf1.

Purpose of the Study:

  • To investigate the interaction between MRGBP and the MRG15 MRG domain.
  • To compare the binding mechanism of MRGBP with that of Pf1.
  • To understand the evolutionary adaptability of MRG domains in binding diverse targets.

Main Methods:

  • Structural biology techniques to analyze protein-protein interactions.
  • Biochemical assays to determine binding affinities.
  • Sequence and structural analysis to compare MRGBP and Pf1.

Main Results:

  • MRGBP binds to the same two surfaces on the MRG15 MRG domain as Pf1.
  • High-affinity binding involves a bipartite structural motif, including an FxLP sequence.
  • MRGBP shows minimal sequence and structural similarity to Pf1 but mimics its interaction pattern.

Conclusions:

  • MRG domains can accommodate structurally diverse proteins like MRGBP and Pf1.
  • The MRG domain's conserved binding surfaces facilitate interactions with various chromatin-associated complexes.
  • This study provides insights into the evolution of protein-protein interactions in chromatin regulation.