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5JXC

SynGAP Coiled-coil trimer

Summary for 5JXC
Entry DOI10.2210/pdb5jxc/pdb
Related5JXB
DescriptorRas/Rap GTPase-activating protein SynGAP (2 entities in total)
Functional Keywordssyngap, coiled-coil, trimer, signaling protein
Biological sourceMus musculus (Mouse)
Total number of polymer chains6
Total formula weight67473.65
Authors
Shang, Y.,Zhang, M. (deposition date: 2016-05-13, release date: 2016-09-28, Last modification date: 2024-03-20)
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 (2.5 Å)
Structure validation

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