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- PDB-1gw4: THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-... -

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Basic information

Entry
Database: PDB / ID: 1gw4
TitleTHE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE
ComponentsAPOA-I
KeywordsHIGH 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 / HDL clearance / spherical high-density lipoprotein particle / Scavenging by Class B Receptors / positive regulation of hydrolase activity / negative regulation of response to cytokine stimulus / protein oxidation / regulation of intestinal cholesterol absorption / vitamin transport ...Defective ABCA1 causes TGD / high-density lipoprotein particle receptor binding / HDL clearance / spherical high-density lipoprotein particle / Scavenging by Class B Receptors / positive regulation of hydrolase activity / negative regulation of response to cytokine stimulus / protein oxidation / regulation of intestinal cholesterol absorption / vitamin transport / cholesterol import / blood vessel endothelial cell migration / high-density lipoprotein particle binding / negative regulation of heterotypic cell-cell adhesion / ABC transporters in lipid homeostasis / apolipoprotein A-I receptor binding / apolipoprotein receptor binding / negative regulation of cytokine production involved in immune response / negative regulation of cell adhesion molecule production / HDL assembly / negative regulation of very-low-density lipoprotein particle remodeling / peptidyl-methionine modification / phosphatidylcholine biosynthetic process / glucocorticoid metabolic process / acylglycerol homeostasis / phosphatidylcholine-sterol O-acyltransferase activator activity / positive regulation of phospholipid efflux / Chylomicron remodeling / positive regulation of cholesterol metabolic process / cellular response to lipoprotein particle stimulus / Chylomicron assembly / : / high-density lipoprotein particle clearance / chylomicron / phospholipid efflux / high-density lipoprotein particle remodeling / phospholipid homeostasis / reverse cholesterol transport / chemorepellent activity / high-density lipoprotein particle assembly / lipid storage / low-density lipoprotein particle / lipoprotein biosynthetic process / cholesterol transfer activity / cholesterol transport / high-density lipoprotein particle / very-low-density lipoprotein particle / regulation of Cdc42 protein signal transduction / triglyceride homeostasis / endothelial cell proliferation / HDL remodeling / cholesterol efflux / Scavenging by Class A Receptors / negative regulation of interleukin-1 beta production / adrenal gland development / negative chemotaxis / cholesterol binding / cholesterol biosynthetic process / positive regulation of Rho protein signal transduction / amyloid-beta formation / endocytic vesicle / positive regulation of cholesterol efflux / negative regulation of tumor necrosis factor-mediated signaling pathway / Scavenging of heme from plasma / Retinoid metabolism and transport / positive regulation of phagocytosis / positive regulation of stress fiber assembly / heat shock protein binding / positive regulation of substrate adhesion-dependent cell spreading / endocytic vesicle lumen / cholesterol metabolic process / cholesterol homeostasis / integrin-mediated signaling pathway / Post-translational protein phosphorylation / Heme signaling / PPARA activates gene expression / phospholipid binding / negative regulation of inflammatory response / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Platelet degranulation / extracellular vesicle / amyloid-beta binding / cytoplasmic vesicle / : / secretory granule lumen / blood microparticle / early endosome / protein stabilization / G protein-coupled receptor signaling pathway / receptor ligand activity / 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
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #20 / Apolipoprotein A/E / : / Apolipoprotein A1/A4/E domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / DISTANCE GEOMETRY CALCULATIONS USING NOE-DERIVED DISTANCES
AuthorsWang, G. / Sparrow, J.T. / Cushley, R.J.
CitationJournal: 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
DepositionJun 4, 1997Processing site: BNL
Revision 1.0Jul 23, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: APOA-I


Theoretical massNumber of molelcules
Total (without water)5,1521
Polymers5,1521
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 50LOWER OPTIMIZATION ERROR AND NO DISTANCE VIOLATION GREATER THAN 0.5 A)
Representative

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Components

#1: Protein/peptide APOA-I / APOLIPOPROTEIN A-I


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

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131DQF-COSY

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Sample preparation

Sample conditionspH: 4.9 / Temperature: 323 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
DGIIHAVELrefinement
DGIIstructure solution
RefinementMethod: DISTANCE GEOMETRY CALCULATIONS USING NOE-DERIVED DISTANCES
Software ordinal: 1
NMR ensembleConformer selection criteria: LOWER OPTIMIZATION ERROR AND NO DISTANCE VIOLATION GREATER THAN 0.5 A)
Conformers calculated total number: 50 / Conformers submitted total number: 1

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