+Open data
-Basic information
Entry | Database: PDB / ID: 2low | ||||||
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Title | Solution structure of AR55 in 50% HFIP | ||||||
Components | Apelin receptor | ||||||
Keywords | MEMBRANE PROTEIN | ||||||
Function / homology | Function and homology information apelin receptor activity / apelin receptor signaling pathway / regulation of gap junction assembly / positive regulation of inhibitory G protein-coupled receptor phosphorylation / vascular associated smooth muscle cell differentiation / atrioventricular valve development / regulation of body fluid levels / venous blood vessel development / positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / endocardial cushion formation ...apelin receptor activity / apelin receptor signaling pathway / regulation of gap junction assembly / positive regulation of inhibitory G protein-coupled receptor phosphorylation / vascular associated smooth muscle cell differentiation / atrioventricular valve development / regulation of body fluid levels / venous blood vessel development / positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / endocardial cushion formation / adult heart development / coronary vasculature development / vasculature development / negative regulation of cAMP-mediated signaling / aorta development / ventricular septum morphogenesis / heart looping / blood vessel development / gastrulation / vasculogenesis / Peptide ligand-binding receptors / positive regulation of release of sequestered calcium ion into cytosol / G protein-coupled receptor activity / positive regulation of angiogenesis / signaling receptor activity / heart development / G alpha (i) signalling events / regulation of gene expression / angiogenesis / G protein-coupled receptor signaling pathway / negative regulation of gene expression / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Model details | Extended conformation, model 10 | ||||||
Authors | Langelaan, D.N. / Rainey, J.K. | ||||||
Citation | Journal: J Phys Chem Lett / Year: 2017 Title: Preserved Transmembrane Segment Topology, Structure, and Dynamics in Disparate Micellar Environments. Authors: Langelaan, D.N. / Pandey, A. / Sarker, M. / Rainey, J.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2low.cif.gz | 764.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2low.ent.gz | 644.9 KB | Display | PDB format |
PDBx/mmJSON format | 2low.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lo/2low ftp://data.pdbj.org/pub/pdb/validation_reports/lo/2low | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7306.109 Da / Num. of mol.: 1 / Fragment: UNP residues 1-55 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: APLNR, AGTRL1, APJ / Production host: Escherichia coli (E. coli) / References: UniProt: P35414 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Solution NMR structure of the N-terminus and first transmembrane segment of the apelin receptor solubilised in 50% HFIP/50% water | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: .9 mM [U-99% 13C; U-99% 15N] AR55, 50 % [U-99% 2H] hexafluoroisopropanol, 1 mM DSS, 5 mM [U-99% 2H] DTT, 40 % H2O, 10 % [U-99% 2H] D2O, 50% Hexafluoroisopropanol/40% H2O /10% D2O Solvent system: 50% Hexafluoroisopropanol/40% H2O /10% D2O | ||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: extended conformation | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 40 |