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- PDB-1t34: ROTATION MECHANISM FOR TRANSMEMBRANE SIGNALING BY THE ATRIAL NATR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1t34 | |||||||||
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Title | ROTATION MECHANISM FOR TRANSMEMBRANE SIGNALING BY THE ATRIAL NATRIURETIC PEPTIDE RECEPTOR | |||||||||
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![]() | SIGNALING PROTEIN / MEMBRANE PROTEIN / RECEPTOR-HORMONE COMPLEX / NATRIURETIC PEPTIDE RECEPTOR / GUANYLYL-CYCLASE-COUPLED RECEPTOR / SIGNAL TRANSDUCTION / ROTATION MECHANISM | |||||||||
Function / homology | ![]() negative regulation of collecting lymphatic vessel constriction / Physiological factors / positive regulation of histamine secretion by mast cell / positive regulation of delayed rectifier potassium channel activity / ANPR-A receptor complex / natriuretic peptide receptor activity / mast cell granule / positive regulation of cGMP-mediated signaling / synaptic signaling via neuropeptide / receptor guanylyl cyclase signaling pathway ...negative regulation of collecting lymphatic vessel constriction / Physiological factors / positive regulation of histamine secretion by mast cell / positive regulation of delayed rectifier potassium channel activity / ANPR-A receptor complex / natriuretic peptide receptor activity / mast cell granule / positive regulation of cGMP-mediated signaling / synaptic signaling via neuropeptide / receptor guanylyl cyclase signaling pathway / peptide receptor activity / response to 3-methylcholanthrene / regulation of body fluid levels / neuropeptide receptor binding / regulation of high voltage-gated calcium channel activity / guanylate cyclase / positive regulation of potassium ion export across plasma membrane / cell growth involved in cardiac muscle cell development / cGMP biosynthetic process / regulation of atrial cardiac muscle cell membrane repolarization / guanylate cyclase activity / hormone binding / multicellular organismal-level water homeostasis / sodium ion export across plasma membrane / glycinergic synapse / neuropeptide hormone activity / cardiac muscle hypertrophy in response to stress / negative regulation of systemic arterial blood pressure / hormone receptor binding / cellular response to angiotensin / adenylate cyclase activity / regulation of calcium ion transmembrane transport via high voltage-gated calcium channel / positive regulation of heart rate / dopamine metabolic process / cGMP-mediated signaling / brush border / peptide hormone binding / neuropeptide signaling pathway / positive regulation of cardiac muscle contraction / negative regulation of blood pressure / blood vessel diameter maintenance / cell projection / female pregnancy / negative regulation of smooth muscle cell proliferation / response to insulin / hormone activity / negative regulation of cell growth / regulation of blood pressure / cellular response to hydrogen peroxide / cellular response to mechanical stimulus / vasodilation / protein folding / heart development / perikaryon / cell surface receptor signaling pathway / receptor complex / response to hypoxia / protein kinase activity / intracellular signal transduction / signaling receptor binding / GTP binding / perinuclear region of cytoplasm / protein-containing complex / extracellular space / ATP binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Ogawa, H. / Qiu, Y. / Ogata, C.M. / Misono, K.S. | |||||||||
![]() | ![]() Title: Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction Authors: Ogawa, H. / Qiu, Y. / Ogata, C.M. / Misono, K.S. #1: ![]() Title: Crystallization and preliminary x-ray analysis of atrial natriuretic peptide (anp) receptor extracellular domain complex with anp: use of ammonium sulfate as the cryosalt Authors: Ogawa, H. / Zhang, X. / Qiu, Y. / Ogata, C.M. / Misono, K.S. #2: ![]() Title: Constitutive activation and uncoupling of the atrial natriuretic peptide receptor by mutations at the dimer interface: role of dimer interface in signaling Authors: Qiu, Y. / Ogawa, H. / Miyagi, M. / Misono, K.S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 182.5 KB | Display | ![]() |
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PDB format | ![]() | 146.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 645.3 KB | Display | ![]() |
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Full document | ![]() | 676 KB | Display | |
Data in XML | ![]() | 21.8 KB | Display | |
Data in CIF | ![]() | 32.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1dp4S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 48434.828 Da / Num. of mol.: 2 / Fragment: HORMONE BINDING DOMAIN (RESIDUES 1-435) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | | Mass: 2217.515 Da / Num. of mol.: 1 / Fragment: RESIDUES 129-149 / Source method: obtained synthetically / Details: This sequence occurs in Rattus norvegicus / References: UniProt: P01161 #3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #4: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 67 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.5 Details: AMMONIUM SULFATE, SODIUM CHLORIDE, pH 6.5, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: SBC-2 / Detector: CCD / Date: Mar 22, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979338 Å / Relative weight: 1 |
Reflection | Resolution: 2.95→87.71 Å / Num. all: 30886 / Num. obs: 25503 / % possible obs: 93.7 % / Observed criterion σ(I): 0.5 / Rmerge(I) obs: 0.054 / Net I/σ(I): 30.9 |
Reflection shell | Resolution: 2.95→3.04 Å / Rmerge(I) obs: 0.554 / Mean I/σ(I) obs: 3.2 / % possible all: 89.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1DP4 Resolution: 2.95→87.71 Å / Cor.coef. Fo:Fc: 0.914 / Cor.coef. Fo:Fc free: 0.902 / SU B: 20.514 / SU ML: 0.378 / Cross valid method: THROUGHOUT / σ(F): 1 / ESU R Free: 0.445 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 52.512 Å2
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Refinement step | Cycle: LAST / Resolution: 2.95→87.71 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.95→3.05 Å / Total num. of bins used: 15 /
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