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

2.4K
2.4K

You might also read

Related Articles

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

Sort by
Same author

Arginine Di-methylation of RIP3 safeguards necroptosis for intestinal homeostasis.

Cell death and differentiation·2026
Same author

Moonlighting cytosolic function of ACAD9: suppression of TRAF6-mediated osteoclastogenesis and protection against osteoporosis.

Cell death & disease·2026
Same author

Inducible CD147 up-regulation boosts extended SARS-CoV-2 infection triggering severe COVID-19 independent of ACE2.

Signal transduction and targeted therapy·2026
Same author

Molecular insight into pemetrexed as a partial agonist of PPAR<sub>γ</sub> through molecular dynamics simulations.

Physical chemistry chemical physics : PCCP·2025
Same author

CMKLR1/PKA signaling reinforces sonic hedgehog pathway to promote medulloblastoma pathogenesis.

Oncogenesis·2025
Same author

Insights into the chirality-dependent recognition of Danshensu Bingpian Zhi stereoisomers with PPAR<sub>γ</sub>.

Physical chemistry chemical physics : PCCP·2024

Related Experiment Video

Updated: Sep 26, 2025

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection
10:02

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection

Published on: February 18, 2014

9.1K

TAB1 binding induced p38α conformation change: an accelerated molecular dynamics simulation study.

Yongjian Zang1, He Wang1, Ying Kang1

  • 1MOE Key Laboratory for Nonequilibrium Synthesis and Modulation of Condensed Matter, School of Physics, Xi'an Jiaotong University, Xi'an 710049, China. yzws-123@xjtu.edu.cn.

Physical Chemistry Chemical Physics : PCCP
|April 20, 2022
PubMed
Summary

TGFβ-activated kinase 1 binding protein 1 (TAB1) binding induces p38α kinase autophosphorylation in myocardial ischemia. Understanding these conformational changes aids in developing targeted p38α inhibitors for ischemic injury treatment.

More Related Videos

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
05:57

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

532
Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

1.4K

Related Experiment Videos

Last Updated: Sep 26, 2025

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection
10:02

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection

Published on: February 18, 2014

9.1K
Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
05:57

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

532
Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

1.4K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiovascular Research

Background:

  • p38α mitogen-activated protein kinase (MAPK) plays a crucial role in cellular responses, including those in myocardial ischemia.
  • Autophosphorylation of p38α is a key regulatory step, often influenced by binding partners like TGFβ-activated kinase 1 binding protein 1 (TAB1).
  • Understanding the structural dynamics of p38α during TAB1-induced activation is vital for developing therapeutic strategies against myocardial ischemia.

Purpose of the Study:

  • To investigate the conformational transformations of p38α upon TAB1 binding using advanced computational methods.
  • To characterize the structural basis of p38α autophosphorylation induced by TAB1.
  • To identify potential targets for selective p38α inhibitors to treat myocardial ischemia.

Main Methods:

  • All-atom accelerated molecular dynamics (MD) simulations were employed to model p38α-TAB1 interactions.
  • Principal component analysis (PCA) was utilized to analyze the large-scale conformational changes observed in the MD simulations.
  • Key structural elements, including the activation loop (A-loop) and helical regions, were examined for dynamic alterations.

Main Results:

  • TAB1 binding induced significant conformational changes in p38α, characterized by the repositioning of the A-loop.
  • A novel intermediate state of p38α with an extended and phosphorylated A-loop was identified.
  • TAB1 binding enhanced intramolecular correlations within p38α, particularly involving the A-loop, αC helix, and L16-loop, with phosphorylation further strengthening these interactions.

Conclusions:

  • The study elucidates the molecular mechanisms underlying TAB1-mediated p38α autophosphorylation and conformational changes.
  • The findings provide insights into the regulation of kinase activity and allosteric communication within p38α.
  • This research facilitates the design of selective p38α inhibitors for therapeutic intervention in myocardial ischemia and related conditions.