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5JXB

PSD-95 extended PDZ3 in complex with SynGAP PBM

Summary for 5JXB
Entry DOI10.2210/pdb5jxb/pdb
DescriptorDisks large homolog 4,SynGAP (2 entities in total)
Functional Keywordspsd-95, pdz, syngap, extension, cell adhesion
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight26815.98
Authors
Shang, Y.,Zhang, M. (deposition date: 2016-05-13, release date: 2016-09-28, Last modification date: 2024-10-16)
Primary citationZeng, M.,Shang, Y.,Araki, Y.,Guo, T.,Huganir, R.L.,Zhang, M.
Phase Transition in Postsynaptic Densities Underlies Formation of Synaptic Complexes and Synaptic Plasticity.
Cell, 166:1163-1175.e12, 2016
Cited by
PubMed Abstract: Postsynaptic densities (PSDs) are membrane semi-enclosed, submicron protein-enriched cellular compartments beneath postsynaptic membranes, which constantly exchange their components with bulk aqueous cytoplasm in synaptic spines. Formation and activity-dependent modulation of PSDs is considered as one of the most basic molecular events governing synaptic plasticity in the nervous system. In this study, we discover that SynGAP, one of the most abundant PSD proteins and a Ras/Rap GTPase activator, forms a homo-trimer and binds to multiple copies of PSD-95. Binding of SynGAP to PSD-95 induces phase separation of the complex, forming highly concentrated liquid-like droplets reminiscent of the PSD. The multivalent nature of the SynGAP/PSD-95 complex is critical for the phase separation to occur and for proper activity-dependent SynGAP dispersions from the PSD. In addition to revealing a dynamic anchoring mechanism of SynGAP at the PSD, our results also suggest a model for phase-transition-mediated formation of PSD.
PubMed: 27565345
DOI: 10.1016/j.cell.2016.07.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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