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- PDB-1le2: STRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HU... -

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Basic information

Entry
Database: PDB / ID: 1le2
TitleSTRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HUMAN APOLIPOPROTEIN-E
ComponentsAPOLIPOPROTEIN E2
KeywordsLIPOPROTEIN
Function / homology
Function and homology information


lipid transport involved in lipid storage / maintenance of location in cell / intermediate-density lipoprotein particle clearance / positive regulation of lipid transport across blood-brain barrier / regulation of cellular response to very-low-density lipoprotein particle stimulus / metal chelating activity / triglyceride-rich lipoprotein particle clearance / negative regulation of triglyceride metabolic process / discoidal high-density lipoprotein particle / Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors ...lipid transport involved in lipid storage / maintenance of location in cell / intermediate-density lipoprotein particle clearance / positive regulation of lipid transport across blood-brain barrier / regulation of cellular response to very-low-density lipoprotein particle stimulus / metal chelating activity / triglyceride-rich lipoprotein particle clearance / negative regulation of triglyceride metabolic process / discoidal high-density lipoprotein particle / Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors / chylomicron remnant clearance / negative regulation of cholesterol biosynthetic process / chylomicron remnant / lipoprotein particle / regulation of amyloid-beta clearance / intermediate-density lipoprotein particle / NMDA glutamate receptor clustering / very-low-density lipoprotein particle remodeling / Chylomicron clearance / acylglycerol homeostasis / phosphatidylcholine-sterol O-acyltransferase activator activity / positive regulation of phospholipid efflux / lipid carrier activity / positive regulation of low-density lipoprotein particle receptor catabolic process / Chylomicron remodeling / cellular response to lipoprotein particle stimulus / very-low-density lipoprotein particle clearance / Chylomicron assembly / high-density lipoprotein particle clearance / phospholipid efflux / lipoprotein catabolic process / very-low-density lipoprotein particle receptor binding / regulation of protein metabolic process / chylomicron / high-density lipoprotein particle remodeling / multivesicular body, internal vesicle / positive regulation of amyloid-beta clearance / reverse cholesterol transport / positive regulation of cholesterol metabolic process / regulation of amyloid fibril formation / high-density lipoprotein particle assembly / host-mediated activation of viral process / lipoprotein biosynthetic process / melanosome organization / cholesterol transfer activity / regulation of behavioral fear response / low-density lipoprotein particle / cholesterol catabolic process / protein import / high-density lipoprotein particle / very-low-density lipoprotein particle / low-density lipoprotein particle remodeling / amyloid precursor protein metabolic process / response to caloric restriction / heparan sulfate proteoglycan binding / negative regulation of amyloid fibril formation / synaptic transmission, cholinergic / regulation of Cdc42 protein signal transduction / regulation of amyloid precursor protein catabolic process / positive regulation of membrane protein ectodomain proteolysis / negative regulation of endothelial cell migration / HDL remodeling / artery morphogenesis / negative regulation of protein metabolic process / cholesterol efflux / regulation of cholesterol metabolic process / regulation of axon extension / Scavenging by Class A Receptors / triglyceride metabolic process / triglyceride homeostasis / low-density lipoprotein particle receptor binding / positive regulation of amyloid fibril formation / virion assembly / regulation of innate immune response / negative regulation of endothelial cell proliferation / negative regulation of platelet-derived growth factor receptor signaling pathway / antioxidant activity / positive regulation of lipoprotein transport / response to dietary excess / positive regulation of dendritic spine development / negative regulation of amyloid-beta formation / lipoprotein particle binding / AMPA glutamate receptor clustering / negative regulation of long-term synaptic potentiation / negative regulation of blood vessel endothelial cell migration / negative regulation of platelet activation / locomotory exploration behavior / negative regulation of blood coagulation / negative regulation of protein secretion / positive regulation of cholesterol efflux / positive regulation of dendritic spine maintenance / fatty acid homeostasis / intracellular transport / regulation of protein-containing complex assembly / positive regulation of endocytosis / regulation of neuronal synaptic plasticity / long-chain fatty acid transport / Nuclear signaling by ERBB4 / positive regulation of lipid biosynthetic process / Retinoid metabolism and transport
Similarity search - Function
Apolipoprotein / Apolipoprotein A/E / : / Apolipoprotein A1/A4/E domain / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 3 Å
AuthorsWilson, C. / Agard, D.A.
Citation
Journal: Structure / Year: 1994
Title: Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein.
Authors: Wilson, C. / Mau, T. / Weisgraber, K.H. / Wardell, M.R. / Mahley, R.W. / Agard, D.A.
#1: Journal: Science / Year: 1991
Title: Three-Dimensional Structure of the Ldl Receptor-Binding Domain of Human Apolipoprotein E
Authors: Wilson, C. / Wardell, M.R. / Weisgraber, K.H. / Mahley, R.W. / Agard, D.A.
#2: Journal: J.Mol.Biol. / Year: 1988
Title: Crystallization and Preliminary X-Ray Diffraction Studies on the Amino-Terminal (Receptor-Binding) Domain of Human Apolipoprotein E3 from Serum Very Low Density Lipoproteins
Authors: Aggerbeck, L.P. / Wetterau, J.R. / Weisgraber, K.H. / Mahley, R.W. / Agard, D.A.
History
DepositionAug 22, 1991Processing site: BNL
Revision 1.0Oct 15, 1992Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: APOLIPOPROTEIN E2


Theoretical massNumber of molelcules
Total (without water)16,6891
Polymers16,6891
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)41.060, 53.940, 83.910
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein APOLIPOPROTEIN E2


Mass: 16689.027 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: E2 / Production host: unidentified (others) / References: UniProt: P02649
Compound detailsTHREE ISOFORMS OF APO-E ARE RELATIVELY COMMON. THE APO-E2 ISOFORM DIFFERS FROM THE WILD-TYPE (E3) ...THREE ISOFORMS OF APO-E ARE RELATIVELY COMMON. THE APO-E2 ISOFORM DIFFERS FROM THE WILD-TYPE (E3) PROTEIN BY THE MUTATION ARG158-->CYS. THE MUTANT PROTEIN SHOWS NORMAL LIPOPROTEIN BINDING BUT LESS THAN 2% OF NORMAL LDL RECEPTOR BINDING. THE STRUCTURE OF THE E2 MUTANT WAS DETERMINED USING STARTING PHASES OBTAINED FOR THE E3 PROTEIN. SECONDARY STRUCTURE WAS ASSIGNED USING THE *DEFINE* PROGRAM (RICHARDS AND KUNDROT, PROTEINS V. 3, 71 (1988)).

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.78 Å3/Da / Density % sol: 55.81 %
Crystal grow
*PLUS
pH: 5.3 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
215 %PEG4001reservior
320 mMsodium acetate1reservoir
40.2 %beta-n-octylglucopyranoide1reservoir
50.1 %beta-mercaptoethanol1reservoir
1protein1drop

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 3 Å / Lowest resolution: 10 Å / Num. obs: 2749 / % possible obs: 67.9 %

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Processing

SoftwareName: X-PLOR / Classification: refinement
RefinementRfactor Rwork: 0.195 / Highest resolution: 3 Å
Details: THE LOOP CONNECTING THE SECOND AND THIRD HELICES OF THE FOUR-HELIX BUNDLE (RESIDUES 83-88) IS POORLY DEFINED IN THE ELECTRON DENSITY MAP. X-PLOR-REFINED COORDINATES FOR THE LOOP HAVE BEEN ...Details: THE LOOP CONNECTING THE SECOND AND THIRD HELICES OF THE FOUR-HELIX BUNDLE (RESIDUES 83-88) IS POORLY DEFINED IN THE ELECTRON DENSITY MAP. X-PLOR-REFINED COORDINATES FOR THE LOOP HAVE BEEN INCLUDED IN THE STRUCTURE BUT ARE LIKELY TO CONTAIN ERRORS.
Refinement stepCycle: LAST / Highest resolution: 3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1167 0 0 0 1167
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.016
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg3.7
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Lowest resolution: 8 Å / Num. reflection obs: 2749 / σ(I): 2 / Rfactor Rwork: 0.195
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Type: x_angle_d / Dev ideal: 3.7

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