PDBsum entry 5jxb

Cell adhesion

PDB id: 5jxb

Contents

Protein chains

117 a.a.

Waters ×4

PDB id:

5jxb

Name:

Cell adhesion

Title:

Psd-95 extended pdz3 in complex with syngap pbm

Structure:

Disks large homolog 4,syngap. Chain: a, c. Synonym: postsynaptic density protein 95,psd-95,synapse-associated protein 90,sap90. Engineered: yes. Other_details: the fusion protein of psd-95 (pdz3 residues 306-410), linker (gsgs), and syngap (residues 415-426)

Source:

Homo sapiens, mus musculus. Human. Organism_taxid: 9606, 10090. Gene: dlg4, psd95. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

2.90Å R-factor: 0.241 R-free: 0.287

Authors:

Y.Shang,M.Zhang

Key ref:

M.Zeng et al. (2016). Phase Transition in Postsynaptic Densities Underlies Formation of Synaptic Complexes and Synaptic Plasticity. Cell, 166, 1163. PubMed id: 27565345

Date:

13-May-16 Release date: 28-Sep-16

Protein chains

J3QQ18  (J3QQ18_MOUSE) -  Synaptic Ras GTPase activating protein 1 homolog (rat) from Mus musculus

Seq: 1308 a.a.

Struc: 117 a.a.*

Protein chains

P78352  (DLG4_HUMAN) -  Disks large homolog 4 from Homo sapiens

Seq: 724 a.a.

Struc: 117 a.a.*

* PDB and UniProt seqs differ at 108 residue positions (black crosses)

Cell 166:1163 (2016)

PubMed id: 27565345

Phase Transition in Postsynaptic Densities Underlies Formation of Synaptic Complexes and Synaptic Plasticity.

M.Zeng, Y.Shang, Y.Araki, T.Guo, R.L.Huganir, M.Zhang.

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.