[English] 日本語
Yorodumi- PDB-1sg1: Crystal Structure of the Receptor-Ligand Complex between Nerve Gr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1sg1 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal Structure of the Receptor-Ligand Complex between Nerve Growth Factor and the Common Neurotrophin Receptor p75 | ||||||
Components |
| ||||||
Keywords | HORMONE/GROWTH FACTOR/MEMBRANE PROTEIN / Nerve Growth Factor / NGF / p75 / Neurotrophin / common neurotrophin receptor / growth factor receptor / receptor-ligand complex / HORMONE-GROWTH FACTOR-MEMBRANE PROTEIN COMPLEX | ||||||
Function / homology | Function and homology information Regulated proteolysis of p75NTR / NFG and proNGF binds to p75NTR / NADE modulates death signalling / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / NFG and proNGF binds to p75NTR / NRIF signals cell death from the nucleus / NF-kB is activated and signals survival / detection of temperature stimulus / dorsal aorta development ...Regulated proteolysis of p75NTR / NFG and proNGF binds to p75NTR / NADE modulates death signalling / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / NFG and proNGF binds to p75NTR / NRIF signals cell death from the nucleus / NF-kB is activated and signals survival / detection of temperature stimulus / dorsal aorta development / p75NTR recruits signalling complexes / Ceramide signalling / death receptor activity / nerve growth factor receptor binding / preprotein binding / positive regulation of odontogenesis of dentin-containing tooth / negative regulation of hair follicle development / NGF processing / positive regulation of synaptic transmission, cholinergic / TRKA activation by NGF / negative regulation of fibroblast growth factor receptor signaling pathway / PLC-gamma1 signalling / Signalling to STAT3 / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / p75NTR negatively regulates cell cycle via SC1 / neurotrophin binding / negative regulation of dendritic spine development / metalloendopeptidase inhibitor activity / positive regulation of myelination / nerve growth factor signaling pathway / nerve development / Retrograde neurotrophin signalling / Axonal growth stimulation / clathrin-coated endocytic vesicle / positive regulation of collateral sprouting / nerve growth factor binding / NADE modulates death signalling / Signalling to p38 via RIT and RIN / peripheral nervous system development / neurotrophin TRKA receptor binding / ARMS-mediated activation / positive regulation of neural precursor cell proliferation / positive regulation of Ras protein signal transduction / regulation of reactive oxygen species metabolic process / negative regulation of mitochondrial depolarization / PI3K/AKT activation / skin development / regulation of neuron differentiation / hair follicle morphogenesis / positive regulation of Rho protein signal transduction / Frs2-mediated activation / neuronal cell body membrane / NRAGE signals death through JNK / skeletal muscle cell differentiation / intracellular glucose homeostasis / odontogenesis of dentin-containing tooth / positive regulation of excitatory postsynaptic potential / Rho protein signal transduction / extrinsic apoptotic signaling pathway via death domain receptors / hair follicle development / Signalling to RAS / fibroblast growth factor receptor signaling pathway / positive regulation of DNA binding / coreceptor activity / dendrite membrane / p75NTR recruits signalling complexes / presynaptic modulation of chemical synaptic transmission / positive regulation of neuron differentiation / NF-kB is activated and signals survival / NRIF signals cell death from the nucleus / negative regulation of angiogenesis / positive regulation of synaptic transmission, glutamatergic / negative regulation of cell migration / neuron projection morphogenesis / central nervous system development / positive regulation of apoptotic signaling pathway / endosome lumen / cell surface receptor protein tyrosine kinase signaling pathway / axon guidance / intracellular protein transport / growth factor activity / circadian regulation of gene expression / modulation of chemical synaptic transmission / neuromuscular junction / memory / small GTPase binding / positive regulation of neuron projection development / positive regulation of miRNA transcription / Golgi lumen / positive regulation of protein localization to nucleus / circadian rhythm / cellular response to amyloid-beta / positive regulation of fibroblast proliferation / cell-cell junction / synaptic vesicle / presynapse / positive regulation of peptidyl-serine phosphorylation / negative regulation of neuron projection development / glucose homeostasis / presynaptic membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.4 Å | ||||||
Authors | He, X.L. / Garcia, K.C. | ||||||
Citation | Journal: Science / Year: 2004 Title: Structure of nerve growth factor complexed with the shared neurotrophin receptor p75 Authors: He, X.L. / Garcia, K.C. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1sg1.cif.gz | 92.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1sg1.ent.gz | 69.4 KB | Display | PDB format |
PDBx/mmJSON format | 1sg1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sg/1sg1 ftp://data.pdbj.org/pub/pdb/validation_reports/sg/1sg1 | HTTPS FTP |
---|
-Related structure data
Related structure data | 1wwwS S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 13515.410 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NGFB / Production host: Escherichia coli (E. coli) / References: UniProt: P01138 #2: Protein | | Mass: 17258.014 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: p75 / Plasmid: pAcGP67A / Production host: unidentified baculovirus / Strain (production host): Tn5 / References: UniProt: P07174 #3: Chemical | ChemComp-CL / | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.3 % |
---|---|
Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 6.3 Details: PEG 1000, isoproponal, sodium chloride, citrate, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1.0597 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Oct 5, 2003 / Details: null |
Radiation | Monochromator: null / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0597 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. all: 16891 / Num. obs: 16891 / % possible obs: 99 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Biso Wilson estimate: 45 Å2 / Rmerge(I) obs: 0.083 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2.4→2.5 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.349 / Mean I/σ(I) obs: 2.4 / % possible all: 97.3 |
-Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MIR Starting model: part of the structure starts from PDB ENTRY 1WWW Resolution: 2.4→50 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||
Displacement parameters | Biso mean: 50.4 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.4→2.49 Å
|