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Yorodumi- PDB-1u34: 3D NMR structure of the first extracellular domain of CRFR-2beta,... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1u34 | ||||||
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Title | 3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor | ||||||
Components | Corticotropin releasing factor receptor 2 | ||||||
Keywords | SIGNALING PROTEIN / Beta sheets and Loops | ||||||
Function / homology | Function and homology information gastric motility / corticotropin-releasing hormone receptor activity / negative regulation of defecation / Class B/2 (Secretin family receptors) / corticotrophin-releasing factor receptor activity / negative regulation of follicle-stimulating hormone secretion / skeletal muscle tissue growth / negative regulation of norepinephrine secretion / positive regulation of serotonin secretion / negative regulation of luteinizing hormone secretion ...gastric motility / corticotropin-releasing hormone receptor activity / negative regulation of defecation / Class B/2 (Secretin family receptors) / corticotrophin-releasing factor receptor activity / negative regulation of follicle-stimulating hormone secretion / skeletal muscle tissue growth / negative regulation of norepinephrine secretion / positive regulation of serotonin secretion / negative regulation of luteinizing hormone secretion / G alpha (s) signalling events / negative regulation of epinephrine secretion / catecholamine biosynthetic process / varicosity / negative regulation of calcium ion import / cell body fiber / positive regulation of cAMP-mediated signaling / positive regulation of stress-activated MAPK cascade / positive regulation of blood pressure / G protein-coupled peptide receptor activity / : / negative regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of heart rate / positive regulation of DNA biosynthetic process / negative regulation of feeding behavior / peptide hormone binding / epithelial cell differentiation / regulation of ERK1 and ERK2 cascade / negative regulation of angiogenesis / axon terminus / actin filament organization / long-term synaptic potentiation / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / hormone activity / positive regulation of interleukin-6 production / perikaryon / cell surface receptor signaling pathway / G protein-coupled receptor signaling pathway / axon / negative regulation of gene expression / neuronal cell body / dendrite / positive regulation of gene expression / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics | ||||||
Authors | Grace, C.R. / Perrin, M.H. / DiGruccio, M.R. / Miller, C.L. / Rivier, J.E. / Vale, W.W. / Riek, R. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor Authors: Grace, C.R. / Perrin, M.H. / DiGruccio, M.R. / Miller, C.L. / Rivier, J.E. / Vale, W.W. / Riek, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1u34.cif.gz | 666.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1u34.ent.gz | 571.1 KB | Display | PDB format |
PDBx/mmJSON format | 1u34.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1u34_validation.pdf.gz | 343.6 KB | Display | wwPDB validaton report |
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Full document | 1u34_full_validation.pdf.gz | 509.7 KB | Display | |
Data in XML | 1u34_validation.xml.gz | 60.4 KB | Display | |
Data in CIF | 1u34_validation.cif.gz | 77.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/u3/1u34 ftp://data.pdbj.org/pub/pdb/validation_reports/u3/1u34 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13626.097 Da / Num. of mol.: 1 / Fragment: ECD1 of CRFR2b Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: Q60748 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The NOEs for structure calculation were taken from 3D and 2D NOESY experiments |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0.2mM in 10mM BisTris(HCl) / pH: 7.4 / Pressure: Ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 700 MHz |
-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics Software ordinal: 1 Details: A total of 1089 meaningful distance restraints and 362 angle restraints were used as an input in the program CYANA followed by restrained energy minimisation using INSIGHT. | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |