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Yorodumi- PDB-1gw3: THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gw3 | ||||||
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Title | THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE | ||||||
Components | APOA-I | ||||||
Keywords | HIGH DENSITY LIPOPROTEINS / KEY IN VIVO COFACTOR FOR THE ENZYME LECITHIN-CHOLESTEROL TRANSFERASE / CHOLESTEROL EFFLUX / RECEPTOR BINDING / AMPHIPATHIC HELICES / HELIX-HINGE-HELIX MOTIF | ||||||
Function / homology | Function and homology information Defective ABCA1 causes TGD / high-density lipoprotein particle receptor binding / Scavenging by Class B Receptors / HDL clearance / spherical high-density lipoprotein particle / positive regulation of hydrolase activity / regulation of intestinal cholesterol absorption / negative regulation of response to cytokine stimulus / protein oxidation / vitamin transport ...Defective ABCA1 causes TGD / high-density lipoprotein particle receptor binding / Scavenging by Class B Receptors / HDL clearance / spherical high-density lipoprotein particle / positive regulation of hydrolase activity / regulation of intestinal cholesterol absorption / negative regulation of response to cytokine stimulus / protein oxidation / vitamin transport / high-density lipoprotein particle binding / cholesterol import / ABC transporters in lipid homeostasis / negative regulation of heterotypic cell-cell adhesion / blood vessel endothelial cell migration / apolipoprotein receptor binding / negative regulation of cell adhesion molecule production / negative regulation of cytokine production involved in immune response / apolipoprotein A-I receptor binding / HDL assembly / peptidyl-methionine modification / negative regulation of very-low-density lipoprotein particle remodeling / phosphatidylcholine biosynthetic process / glucocorticoid metabolic process / Chylomicron remodeling / phosphatidylcholine-sterol O-acyltransferase activator activity / phosphatidylcholine metabolic process / positive regulation of phospholipid efflux / lipid storage / phospholipid homeostasis / Chylomicron assembly / positive regulation of cholesterol metabolic process / high-density lipoprotein particle remodeling / high-density lipoprotein particle clearance / phospholipid efflux / cholesterol transfer activity / reverse cholesterol transport / cholesterol transport / chemorepellent activity / high-density lipoprotein particle assembly / very-low-density lipoprotein particle / positive regulation of CoA-transferase activity / lipoprotein biosynthetic process / high-density lipoprotein particle / endothelial cell proliferation / regulation of Cdc42 protein signal transduction / triglyceride homeostasis / HDL remodeling / cholesterol efflux / Scavenging by Class A Receptors / cholesterol binding / negative regulation of interleukin-1 beta production / positive regulation of Rho protein signal transduction / negative chemotaxis / adrenal gland development / cholesterol biosynthetic process / endocytic vesicle / positive regulation of cholesterol efflux / negative regulation of tumor necrosis factor-mediated signaling pathway / Scavenging of heme from plasma / positive regulation of phagocytosis / positive regulation of substrate adhesion-dependent cell spreading / Retinoid metabolism and transport / positive regulation of stress fiber assembly / endocytic vesicle lumen / heat shock protein binding / cholesterol metabolic process / cholesterol homeostasis / integrin-mediated signaling pathway / Post-translational protein phosphorylation / regulation of protein phosphorylation / phospholipid binding / Heme signaling / PPARA activates gene expression / negative regulation of inflammatory response / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / extracellular vesicle / Platelet degranulation / amyloid-beta binding / cytoplasmic vesicle / collagen-containing extracellular matrix / secretory granule lumen / blood microparticle / protein stabilization / early endosome / G protein-coupled receptor signaling pathway / Amyloid fiber formation / endoplasmic reticulum lumen / signaling receptor binding / enzyme binding / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY CALCULATIONS USING NOE-DERIVED DISTANCES | ||||||
Authors | Wang, G. / Sparrow, J.T. / Cushley, R.J. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. Authors: Wang, G. / Sparrow, J.T. / Cushley, R.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gw3.cif.gz | 20.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gw3.ent.gz | 15 KB | Display | PDB format |
PDBx/mmJSON format | 1gw3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gw/1gw3 ftp://data.pdbj.org/pub/pdb/validation_reports/gw/1gw3 | 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/peptide | Mass: 5151.779 Da / Num. of mol.: 1 / Fragment: RESIDUES 142 - 187 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P02647 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 4.9 / Temperature: 310 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY CALCULATIONS USING NOE-DERIVED DISTANCES Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: LOWER OPTIMIZATION ERROR AND NO DISTANCE VIOLATION GREATER THAN 0.5 A) Conformers calculated total number: 50 / Conformers submitted total number: 1 |