9IUI

Crystal structure of PSD-95 GK domain in complex with GK_FingR

Summary for 9IUI

• Entry DOI: 10.2210/pdb9iui/pdb
• Descriptor: Disks large homolog 4, FingR targeting PSD-95, GLYCEROL, ... (6 entities in total)
• Functional Keywords: protein complex, protein binding
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 4
• Total formula weight: 64977.09

Authors

Zhu, S.,Cai, Q.,Zhang, M. (deposition date: 2024-07-21, release date: 2025-07-23, Last modification date: 2025-09-10)

Primary citation

Jia, B.,Zhu, S.,Shen, Z.,Chen, X.,Li, H.,Zhao, S.,Cai, Q.,Wang, Y.,Wang, Z.,Nicoll, R.A.,Lu, Y.,Zhang, M.
Modulating synaptic glutamate receptors by targeting network nodes of the postsynaptic density condensate.
Mol.Cell, 85:3166-, 2025

PubMed Abstract: Biological condensates are assembled through phase separation and play critical roles in diverse cellular processes. Condensates in cells form percolated molecular networks via multi-valent interactions among biomolecules. How the network properties of a condensate are connected to its biological function is poorly understood. Using the neuronal postsynaptic density (PSD) condensate as a paradigm, we demonstrate thatbiological condensates can be bidirectionally modulated by strengthening or weakening different interaction nodes within the network. The clustering, mobility, and synaptic functions of AMPA receptors are exquisitely sensitive to alterations in the strength and complexity of the PSD condensate molecular network without changing the binding of the receptor to its direct downstream scaffold. Thus, biological condensates are complex systems with emergent network properties that are harnessed for cellular functions and in this case for synaptic plasticity.

PubMed: 40803326
DOI: 10.1016/j.molcel.2025.07.017

Experimental method

X-RAY DIFFRACTION (1.93 Å)