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- PDB-3dxe: Crystal structure of the intracellular domain of human APP (T668A... -

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Basic information

Entry
Database: PDB / ID: 3dxe
TitleCrystal structure of the intracellular domain of human APP (T668A mutant) in complex with Fe65-PTB2
Components
  • Amyloid beta A4 protein
  • Amyloid beta A4 protein-binding family B member 1
KeywordsPROTEIN BINDING / Alzheimer's disease / APP / AICD / Fe65 / PTB domain / Alzheimer disease / Amyloid / Apoptosis / Cell adhesion / Coated pit / Disease mutation / Endocytosis / Glycoprotein / Heparin-binding / Iron / Membrane / Metal-binding / Notch signaling pathway / Phosphoprotein / Protease inhibitor / Proteoglycan / Serine protease inhibitor / Transmembrane
Function / homology
Function and homology information


negative regulation of cell cycle G1/S phase transition / amyloid-beta complex / negative regulation of presynapse assembly / cytosolic mRNA polyadenylation / collateral sprouting in absence of injury / microglia development / proline-rich region binding / regulation of synapse structure or activity / regulation of Wnt signaling pathway / synaptic assembly at neuromuscular junction ...negative regulation of cell cycle G1/S phase transition / amyloid-beta complex / negative regulation of presynapse assembly / cytosolic mRNA polyadenylation / collateral sprouting in absence of injury / microglia development / proline-rich region binding / regulation of synapse structure or activity / regulation of Wnt signaling pathway / synaptic assembly at neuromuscular junction / Formyl peptide receptors bind formyl peptides and many other ligands / axo-dendritic transport / axon midline choice point recognition / smooth endoplasmic reticulum calcium ion homeostasis / astrocyte activation involved in immune response / NMDA selective glutamate receptor signaling pathway / mating behavior / regulation of spontaneous synaptic transmission / ciliary rootlet / Golgi-associated vesicle / low-density lipoprotein particle receptor binding / PTB domain binding / Lysosome Vesicle Biogenesis / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / positive regulation of amyloid fibril formation / neuron remodeling / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / nuclear envelope lumen / COPII-coated ER to Golgi transport vesicle / suckling behavior / signaling receptor activator activity / dendrite development / modulation of excitatory postsynaptic potential / TRAF6 mediated NF-kB activation / presynaptic active zone / positive regulation of protein metabolic process / neuromuscular process controlling balance / Advanced glycosylation endproduct receptor signaling / The NLRP3 inflammasome / negative regulation of long-term synaptic potentiation / smooth muscle contraction / regulation of presynapse assembly / regulation of multicellular organism growth / transition metal ion binding / intracellular copper ion homeostasis / negative regulation of neuron differentiation / ECM proteoglycans / spindle midzone / positive regulation of T cell migration / smooth endoplasmic reticulum / Purinergic signaling in leishmaniasis infection / forebrain development / positive regulation of chemokine production / clathrin-coated pit / Notch signaling pathway / protein serine/threonine kinase binding / positive regulation of G2/M transition of mitotic cell cycle / extracellular matrix organization / neuron projection maintenance / Mitochondrial protein degradation / response to interleukin-1 / ionotropic glutamate receptor signaling pathway / positive regulation of mitotic cell cycle / cholesterol metabolic process / axonogenesis / positive regulation of calcium-mediated signaling / dendritic shaft / platelet alpha granule lumen / adult locomotory behavior / positive regulation of glycolytic process / central nervous system development / learning / positive regulation of interleukin-1 beta production / trans-Golgi network membrane / positive regulation of long-term synaptic potentiation / endosome lumen / positive regulation of protein secretion / locomotory behavior / astrocyte activation / Post-translational protein phosphorylation / positive regulation of JNK cascade / microglial cell activation / regulation of long-term neuronal synaptic plasticity / serine-type endopeptidase inhibitor activity / synapse organization / TAK1-dependent IKK and NF-kappa-B activation / positive regulation of non-canonical NF-kappaB signal transduction / neuromuscular junction / visual learning / recycling endosome / positive regulation of neuron projection development / positive regulation of interleukin-6 production / Golgi lumen / cognition / neuron cellular homeostasis / positive regulation of inflammatory response / endocytosis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / cellular response to amyloid-beta / neuron projection development
Similarity search - Function
Amyloid beta precursor protein binding family B member 1/2/3 / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI domain / Amyloidogenic glycoprotein, copper-binding / Amyloidogenic glycoprotein, copper-binding domain conserved site / Amyloidogenic glycoprotein, copper-binding domain superfamily / Copper-binding of amyloid precursor, CuBD / Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. ...Amyloid beta precursor protein binding family B member 1/2/3 / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI domain / Amyloidogenic glycoprotein, copper-binding / Amyloidogenic glycoprotein, copper-binding domain conserved site / Amyloidogenic glycoprotein, copper-binding domain superfamily / Copper-binding of amyloid precursor, CuBD / Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. / Amyloidogenic glycoprotein, amyloid-beta peptide superfamily / Beta-amyloid peptide (beta-APP) / Amyloidogenic glycoprotein, amyloid-beta peptide / Beta-amyloid precursor protein C-terminal / Amyloidogenic glycoprotein, intracellular domain, conserved site / Beta-amyloid precursor protein C-terminus / Amyloid precursor protein (APP) intracellular domain signature. / Amyloidogenic glycoprotein, extracellular / Amyloidogenic glycoprotein, heparin-binding / Amyloidogenic glycoprotein, E2 domain / E2 domain superfamily / Amyloidogenic glycoprotein, heparin-binding domain superfamily / Amyloid A4 N-terminal heparin-binding / E2 domain of amyloid precursor protein / Amyloid precursor protein (APP) E1 domain profile. / Amyloid precursor protein (APP) E2 domain profile. / amyloid A4 / Amyloidogenic glycoprotein / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / PH-like domain superfamily / Roll / Mainly Beta
Similarity search - Domain/homology
Amyloid beta precursor protein binding family B member 1 / Amyloid-beta precursor protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2 Å
AuthorsRadzimanowski, J. / Sinning, I. / Wild, K.
Citation
Journal: Embo Rep. / Year: 2008
Title: Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2.
Authors: Radzimanowski, J. / Simon, B. / Sattler, M. / Beyreuther, K. / Sinning, I. / Wild, K.
#1: Journal: Acta Crystallogr.,Sect.F / Year: 2008
Title: Overproduction, purification, crystallization and preliminary X-ray analysis of human Fe65-PTB2 in complex with the amyloid precursor protein intracellular domain
Authors: Radzimanowski, J. / Beyreuther, K. / Sinning, I. / Wild, K.
History
DepositionJul 24, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 16, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 1, 2017Group: Database references
Revision 1.3Oct 20, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Feb 21, 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: Amyloid beta A4 protein-binding family B member 1
B: Amyloid beta A4 protein
C: Amyloid beta A4 protein-binding family B member 1
D: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)39,0504
Polymers39,0504
Non-polymers00
Water4,252236
1
A: Amyloid beta A4 protein-binding family B member 1
B: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)19,5252
Polymers19,5252
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2090 Å2
ΔGint-14 kcal/mol
Surface area7950 Å2
MethodPISA
2
C: Amyloid beta A4 protein-binding family B member 1
D: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)19,5252
Polymers19,5252
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2080 Å2
ΔGint-14 kcal/mol
Surface area8190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)115.377, 115.377, 75.523
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number169
Space group name H-MP61
DetailsTHE ASYMMETRIC UNIT CONTAINS TWO COPIES OF A PROTEIN PROTEIN COMPLEX (ONE BIOMOLECULE 1 BINDS ONE BIOMOLECULE 2).

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Components

#1: Protein Amyloid beta A4 protein-binding family B member 1


Mass: 15459.690 Da / Num. of mol.: 2 / Fragment: PTB2 domain, UNP residues 534-667
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APBB1, FE65, RIR / Plasmid: pET21d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL / References: UniProt: O00213
#2: Protein/peptide Amyloid beta A4 protein


Mass: 4065.479 Da / Num. of mol.: 2 / Fragment: APP intracellular domain, UNP residues 739-770 / Mutation: T668A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APP, A4, AD1 / Plasmid: pETtrx_1b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL / References: UniProt: P05067
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 236 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.77 Å3/Da / Density % sol: 67.34 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 4.6
Details: 3.2 M NaCl, 0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.975 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 19, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.975 Å / Relative weight: 1
ReflectionResolution: 2→60 Å / Num. obs: 37351 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 15 % / Rmerge(I) obs: 0.119 / Net I/σ(I): 23.1
Reflection shellResolution: 2→2.11 Å / Redundancy: 15.4 % / Rmerge(I) obs: 0.612 / Mean I/σ(I) obs: 3.1 / % possible all: 95.3

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Processing

Software
NameVersionClassificationNB
REFMAC5.3.0008refinement
PDB_EXTRACT3.006data extraction
DNAdata collection
MOSFLMdata reduction
SCALAdata scaling
SOLVEphasing
RefinementResolution: 2→19.32 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.937 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 3.167 / SU ML: 0.091 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.139 / ESU R Free: 0.136 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.241 1893 5.1 %RANDOM
Rwork0.206 ---
obs0.208 37351 96.66 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 89.4 Å2 / Biso mean: 42.567 Å2 / Biso min: 18.75 Å2
Baniso -1Baniso -2Baniso -3
1-0.01 Å20 Å20 Å2
2--0.01 Å20 Å2
3----0.01 Å2
Refinement stepCycle: LAST / Resolution: 2→19.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2400 0 0 236 2636
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.0222496
X-RAY DIFFRACTIONr_angle_refined_deg1.5691.9333393
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.6245312
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.15323.846117
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.77315396
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.5371514
X-RAY DIFFRACTIONr_chiral_restr0.1130.2372
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.021928
X-RAY DIFFRACTIONr_nbd_refined0.2160.21072
X-RAY DIFFRACTIONr_nbtor_refined0.2950.21693
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1810.2176
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2380.248
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2110.219
X-RAY DIFFRACTIONr_mcbond_it1.3151.51613
X-RAY DIFFRACTIONr_mcangle_it2.04522507
X-RAY DIFFRACTIONr_scbond_it2.70731021
X-RAY DIFFRACTIONr_scangle_it3.9364.5884
LS refinement shellResolution: 2→2.052 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.322 127 -
Rwork0.279 2618 -
all-2745 -
obs--96.96 %

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