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- PDB-1odp: PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH... -

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Entry
Database: PDB / ID: 1odp
TitlePEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.6, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40
ComponentsAPOA-I PEPTIDE
KeywordsLIPID TRANSPORT / APOLIPOPROTEIN A-I / COFACTOR FOR LCAT ACTIVATION
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
Apolipoprotein A/E / Apolipoprotein A1/A4/E domain
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsWang, G. / Treleaven, W.D. / Cushley, R.J.
CitationJournal: Biochim.Biophys.Acta / Year: 1996
Title: Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions.
Authors: Wang, G. / Treleaven, W.D. / Cushley, R.J.
History
DepositionMar 2, 1996Processing site: BNL
Revision 1.0Jun 10, 1996Provider: 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: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: APOA-I PEPTIDE


Theoretical massNumber of molelcules
Total (without water)2,3371
Polymers2,3371
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)5 / 20MOST CLOSELY RESEMBLING THE AVERAGE STRUCTURE OF OF A CALCULATED SET OF 20 CONFORMERS
Representative

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Components

#1: Protein/peptide APOA-I PEPTIDE / APOA-I (166 - 185) / APOLIPOPROTEIN A-I (166 - 185)


Mass: 2336.605 Da / Num. of mol.: 1 / Fragment: RESIDUES 166 - 185
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

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Sample preparation

Sample conditionspH: 6.6 / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR software
NameDeveloperClassification
DGIIHAVELrefinement
DiscoverBIOSYM TECHNOLOGIES, INC.refinement
NMR ensembleConformer selection criteria: MOST CLOSELY RESEMBLING THE AVERAGE STRUCTURE OF OF A CALCULATED SET OF 20 CONFORMERS
Conformers calculated total number: 20 / Conformers submitted total number: 5

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