Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Protein-Protein Interfaces

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

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 to...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

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 to...

Assembly of Signaling Complexes

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,...

You might also read

Related Articles

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

Sort by

Same author

Unveiling acute toxicity trends in nasopharyngeal carcinoma: A global bibliometric perspective.

Journal of visualized experiments : JoVE·2026

Same author

Splicing deficiency is driven by genomic erosion in non-recombining algal mating-type chromosomes.

PLoS biology·2026

Same author

Decoupling of global metabolic flux and proteome partitioning in bacteria.

Science (New York, N.Y.)·2026

Same author

Reverse engineering of BNIP3 identifies a mitochondrial protective peptide.

Nature communications·2026

Same author

The Prognostic Value of Serum Inflammatory Markers in Nasopharyngeal Carcinoma Patients Treated With Immune Checkpoint Inhibitors: A Multicenter Study.

Cancer medicine·2026

Same author

A patient-specific induced pluripotent stem cell and neural stem cell resource for angelman syndrome with 15q11.2-q13 deletion.

Scientific reports·2026

Search research articles

Related Experiment Video

Updated: May 18, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Structural analysis of the quaking homodimerization interface.

Christine Beuck¹, Song Qu, W Samuel Fagg

¹Department of Molecular Biology, Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Journal of Molecular Biology

|September 18, 2012

Summary

This summary is machine-generated.

The Quaking (QkI) protein

More Related Videos

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

Published on: November 2, 2018

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Related Experiment Videos

Last Updated: May 18, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

Published on: November 2, 2018

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

Molecular Biology
Structural Biology
Gene Regulation

Background:

Quaking (QkI) is a STAR protein family member regulating mRNA.
QkI-5's role in non-CNS tissues and STAR protein dimerization is unclear.
STAR proteins bind RNA as dimers, but homodimerization/heterodimerization roles need clarification.

Purpose of the Study:

Determine the structural basis of QkI dimerization.
Investigate the functional importance of QkI homodimerization for RNA binding and gene regulation.

Main Methods:

X-ray crystallography to determine the QkI dimerization domain structure.
In vitro RNA binding assays.
In vivo splicing assays to assess QkI function.

Main Results:

Crystal structure reveals a stacked helix-turn-helix arrangement with an additional helix at the dimer interface.
Interface variability suggests selective homodimerization.
Dimerization-inhibiting mutations impair RNA binding, protein levels, and splicing function.

Conclusions:

A functional QkI homodimerization domain is essential for QkI-5 activity in mammalian cells.
Structural insights explain selective homodimerization within the STAR protein family.