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Related Experiment Video

Updated: Jan 10, 2026

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

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Published on: May 13, 2020

Structural Modeling and Dynamics of the Full-Length Homer1 Multimer.

Zsófia E Kálmán¹, András Czajlik², Brigitta Maruzs¹

¹Faculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.

|November 21, 2025

Summary

This summary is machine-generated.

Homer proteins are key to brain cell communication. This study reveals new insights into Homer1 protein flexibility, suggesting it plays a dynamic role in postsynaptic network organization.

Keywords:

EVH1 domain MD simulation NMR coiled coil dynamics

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Last Updated: Jan 10, 2026

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Area of Science:

Neuroscience
Molecular Biology
Structural Biology

Background:

Homer proteins act as crucial scaffolds in the postsynaptic density, organizing neurotransmitter receptor complexes.
Full-length Homer1 forms a homotetramer, interacting with target proteins via its EVH1 domain and coiled-coil region.

Purpose of the Study:

To determine the atomistic structure and dynamics of the Homer1 coiled coil and EVH1 domains.
To understand how these structural features influence the overall Homer1 tetramer organization and flexibility.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy for EVH1 domain structure and dynamics.
Atomistic modeling and molecular dynamics simulations for the coiled coil region.

Main Results:

NMR ensemble of the EVH1 domain shows subtle differences, indicating potential ligand-induced conformational changes.
Molecular dynamics reveal distinct flexibility patterns in the coiled coil, with the N-terminal segment showing significant motion.
The N-terminal coiled coil's high conservation suggests functional importance of its dynamics.

Conclusions:

The Homer1 tetramer exhibits previously uncharacterized flexibility, particularly in its coiled coil region.
This flexibility may facilitate dynamic rearrangements within the postsynaptic protein network.
These findings offer new perspectives on Homer1's role in synaptic plasticity and function.