SASDGH5: The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + g...

Basic information

• Entry: Database: SASBDB / ID: SASDGH5

Sample

The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH)

• PDZ1-2 fragment of PSD-95/Disks large homolog 4 (protein), PDZ1-2, Homo sapiens

Function / homology

Function:

LGI-ADAM interactions / P2Y1 nucleotide receptor binding / beta-1 adrenergic receptor binding / neuroligin family protein binding / NrCAM interactions / synaptic vesicle maturation / positive regulation of neuron projection arborization / regulation of grooming behavior / receptor localization to synapse / protein localization to synapse / vocalization behavior / cerebellar mossy fiber / cellular response to potassium ion / Synaptic adhesion-like molecules / neuron spine / negative regulation of receptor internalization / AMPA glutamate receptor clustering / Trafficking of AMPA receptors / dendritic spine morphogenesis / establishment or maintenance of epithelial cell apical/basal polarity / juxtaparanode region of axon / neuron projection terminus / postsynaptic neurotransmitter receptor diffusion trapping / acetylcholine receptor binding / RHO GTPases activate CIT / Assembly and cell surface presentation of NMDA receptors / regulation of NMDA receptor activity / Neurexins and neuroligins / Activation of Ca-permeable Kainate Receptor / neurotransmitter receptor localization to postsynaptic specialization membrane / cortical cytoskeleton / Signaling by ERBB4 / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / extrinsic component of cytoplasmic side of plasma membrane / locomotory exploration behavior / AMPA glutamate receptor complex / social behavior / Long-term potentiation / excitatory synapse / neuromuscular process controlling balance / positive regulation of protein tyrosine kinase activity / positive regulation of excitatory postsynaptic potential / D1 dopamine receptor binding / positive regulation of synaptic transmission / ionotropic glutamate receptor binding / Ras activation upon Ca2+ influx through NMDA receptor / dendrite cytoplasm / learning / synaptic membrane / PDZ domain binding / adherens junction / postsynaptic density membrane / regulation of long-term neuronal synaptic plasticity / establishment of protein localization / neuromuscular junction / kinase binding / cell-cell adhesion / endocytic vesicle membrane / cell junction / synaptic vesicle / nervous system development / positive regulation of cytosolic calcium ion concentration / scaffold protein binding / RAF/MAP kinase cascade / protein-containing complex assembly / basolateral plasma membrane / chemical synaptic transmission / protein phosphatase binding / postsynaptic membrane / dendritic spine / postsynaptic density / neuron projection / glutamatergic synapse / synapse / protein-containing complex binding / protein kinase binding / endoplasmic reticulum / signal transduction / plasma membrane / cytosol / cytoplasm

Domain/homology:

Polyubiquitination (PEST) N-terminal domain of MAGUK / Disks large homologue 1, N-terminal PEST domain / Polyubiquitination (PEST) N-terminal domain of MAGUK / PDZ-associated domain of NMDA receptors / PDZ-associated domain of NMDA receptors / Disks large 1-like / : / Guanylate kinase, conserved site / Guanylate kinase-like signature. / Guanylate kinase-like domain profile. / Guanylate kinase-like domain / Guanylate kinase/L-type calcium channel beta subunit / Guanylate kinase / Guanylate kinase homologues. / PDZ domain / SH3 domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / P-loop containing nucleoside triphosphate hydrolase

Component:

Disks large homolog 4

• Biological species: Homo sapiens (human)
• Citation: Date: 2019 Sep 19; Title: How the dual PDZ domain from Postsynaptic density protein 95 clusters ion channels and receptors; Authors: Rodzli N / Lockhart-Cairns M / Levy C / Chipperfield J / Bird L / Baldock C

Contact author

• Stephen Prince (University of Manchester, Manchester, UK)

Models

• Model #3755: ; Type: atomic / Chi-square value: 1.41; Search similar-shape structures of this assembly by Omokage search (details)
• Model #3756: ; Type: atomic / Chi-square value: 1.41; Search similar-shape structures of this assembly by Omokage search (details)
• Model #3757: ; Type: atomic / Chi-square value: 1.41; Search similar-shape structures of this assembly by Omokage search (details)
• Model #3758: ; Type: atomic / Chi-square value: 1.41; Search similar-shape structures of this assembly by Omokage search (details)
• Model #3759: ; Type: atomic / Chi-square value: 1.41; Search similar-shape structures of this assembly by Omokage search (details)
• Model #3760: ; Type: atomic / Chi-square value: 1.41; Search similar-shape structures of this assembly by Omokage search (details)
• Model #3761: ; Type: atomic / Chi-square value: 1.41; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH); Specimen concentration: 7.5 mg/ml
• Buffer: Name: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH / pH: 8.5

Entity #1889

Name: PDZ1-2 / Type: protein
Description: PDZ1-2 fragment of PSD-95/Disks large homolog 4
Formula weight: 20.8 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P78352
Sequence:

GPGTEGEMEY EEITLERGNS GLGFSIAGGT DNPHIGDDPS IFITKIIPGG AAAQDGRLRV NDSILFVNEV DVREVTHSAA VEALKEAGSI VRLYVMRRKP PAEKVMEIKL IKGPKGLGFS IAGGVGNQHI PGDNSIYVTK IIEGGAAHKD GRLQIGDKIL AVNSVGLEDV MHEDAVAALK NTYDVVYLKV AKPSNA

Experimental information

• Beam: Instrument name: Diamond Light Source B21 / City: Didcot / 国: UK / Shape: 1 x 5 mm / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 3.9 mm
• Detector: Name: Pilatus 2M

Scan

Title: The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH)
Measurement date: Sep 16, 2016 / Number of frames: 17 / Unit: 1/A /

	Min	Max
Q	0.0271	0.3998

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 1352 /

	Min	Max
Q	0.0284783	0.399829
P(R) point	1	1352
R	0	63.29

Result

Type of curve: single_conc
Comments: Scattering data are fitted using the ATSAS OLIGOMER program using a suite of models. The ATSAS program FFMAKER was used to generate form factors for each model in the suite. Each model is assigned a volume fraction to fit the observed scattering profile. 3 monomer models are included, the first is a compact conformation of PDZ1-2 similar to PDB entries 6spv/6spz; the other two are domain models obtained from a representative run of the ATSAS EOM program with data projected to infinite dilution. Multimeric models are drawn from a "clustering Spacegroup", unit cell 14.8nm symmetry I2(1)3, and consist of identical copies of an extended conformation of PDZ1-2 (similar to PDB entry 3zrt) assembled by symmetry operations. In the order of deposition: Model number; Stoichiometry; MW (kDa); source; Volume fraction. 1; 1; 21; Crystal Structure; 0.436. 2; 1; 21; EOM; 0.160. 3; 1; 21; EOM; 0.341. 4; 2; 42; clustering Spacegroup; 0.000. 5; 4; 84; clustering Spacegroup; 0.029. 6; 8; 168; clustering Spacegroup; 0.034. 7; 12, 252; clustering Spacegroup; 0.000.

	Experimental	Porod
MW	20.8 kDa	18 kDa
Volume	-	29 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	0.1164	0.1355	0.00021
Radius of gyration, Rg	2.31 nm	2.737 nm	0.046

	Min	Max
D	-	6.33
Guinier point	6	53