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- PDB-2yt1: Solution structure of the chimera of the C-terminal tail peptide ... -

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Basic information

Entry
Database: PDB / ID: 2yt1
TitleSolution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
ComponentsAmyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2
KeywordsPROTEIN BINDING / Chimera / Fe65L / PID domain / amyloid precursor protein / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information


negative regulation of cell cycle phase transition / regulation of response to calcium ion / positive regulation of protein import / Formyl peptide receptors bind formyl peptides and many other ligands / regulation of neurotransmitter uptake / regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway / positive regulation of response to endoplasmic reticulum stress / negative regulation of presynapse assembly / Advanced glycosylation endproduct receptor signaling / positive regulation of gene expression, epigenetic ...negative regulation of cell cycle phase transition / regulation of response to calcium ion / positive regulation of protein import / Formyl peptide receptors bind formyl peptides and many other ligands / regulation of neurotransmitter uptake / regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway / positive regulation of response to endoplasmic reticulum stress / negative regulation of presynapse assembly / Advanced glycosylation endproduct receptor signaling / positive regulation of gene expression, epigenetic / cytosolic mRNA polyadenylation / endosome to plasma membrane transport vesicle / low-density lipoprotein particle mediated signaling / ECM proteoglycans / phospholipase D-activating G protein-coupled receptor signaling pathway / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / regulation of dendritic spine maintenance / negative regulation of blood circulation / positive regulation of endothelin production / positive regulation of Toll signaling pathway / maintenance of lens transparency / TRAF6 mediated NF-kB activation / Lysosome Vesicle Biogenesis / positive regulation of synaptic transmission, cholinergic / positive regulation of long-term synaptic depression / positive regulation of G protein-coupled receptor internalization / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / protein trimerization / smooth endoplasmic reticulum calcium ion homeostasis / response to yeast / G alpha (q) signalling events / TAK1-dependent IKK and NF-kappa-B activation / positive regulation of amyloid precursor protein catabolic process / lipoprotein particle / regulation of amyloid-beta clearance / synaptic assembly at neuromuscular junction / intermediate-density lipoprotein particle / Platelet degranulation / smooth muscle contraction / ciliary rootlet / RAGE receptor binding / antifungal humoral response / G alpha (i) signalling events / regulation of amyloid fibril formation / positive regulation of G protein-coupled receptor signaling pathway / Mitochondrial protein degradation / suckling behavior / low-density lipoprotein particle / high-density lipoprotein particle / very-low-density lipoprotein particle / COPII-coated ER to Golgi transport vesicle / neuromuscular process controlling balance / acetylcholine receptor binding / frizzled binding / amyloid-beta complex / growth cone lamellipodium / cellular response to norepinephrine stimulus / collateral sprouting in absence of injury / growth cone filopodium / heparan sulfate proteoglycan binding / positive regulation of monocyte chemotaxis / microglia development / hippocampal neuron apoptotic process / axo-dendritic transport / positive regulation of membrane protein ectodomain proteolysis / axon midline choice point recognition / regulation of synapse structure or activity / forebrain development / astrocyte activation involved in immune response / positive regulation of extrinsic apoptotic signaling pathway / negative regulation of dendritic spine maintenance / regulation of spontaneous synaptic transmission / mating behavior / negative regulation of neuron differentiation / negative regulation of protein localization to nucleus / growth factor receptor binding / positive regulation of cAMP/PKA signal transduction / presynaptic active zone / peptidase activator activity / positive regulation of amyloid fibril formation / regulation of toll-like receptor signaling pathway / Golgi-associated vesicle / PTB domain binding / astrocyte projection / neuron remodeling / spindle midzone / dendrite development / nuclear envelope lumen / regulation of multicellular organism growth / chemoattractant activity / intracellular vesicle / smooth endoplasmic reticulum / positive regulation of protein metabolic process / negative regulation of Wnt signaling pathway / signaling receptor activator activity / negative regulation of long-term synaptic potentiation / associative learning / regulation of MAPK cascade / apolipoprotein binding
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, heparin-binding / Amyloid A4 N-terminal heparin-binding / 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, E2 domain / E2 domain superfamily / Amyloidogenic glycoprotein, heparin-binding domain superfamily / 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 / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / WW domain / WW/rsp5/WWP domain signature. / PH-domain like / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / PH-like domain superfamily / Roll / Mainly Beta
Similarity search - Domain/homology
Amyloid-beta precursor protein / Amyloid beta precursor protein binding family B member 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsLi, H. / Koshiba, S. / Watanabe, S. / Harada, T. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: J.Biol.Chem. / Year: 2008
Title: Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode
Authors: Li, H. / Koshiba, S. / Hayashi, F. / Tochio, N. / Tomizawa, T. / Kasai, T. / Yabuki, T. / Motoda, Y. / Harada, T. / Watanabe, S. / Inoue, M. / Hayashizaki, Y. / Tanaka, A. / Kigawa, T. / Yokoyama, S.
History
DepositionApr 5, 2007Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 8, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.3May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Remark 650HELIX Determination method: Author determined
Remark 700SHEET Determination method: Author determined

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2


Theoretical massNumber of molelcules
Total (without water)20,0071
Polymers20,0071
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)20 / 100structures with the least restraint violations, target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2


Mass: 20007.113 Da / Num. of mol.: 1 / Fragment: APP peptide and PID domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Description: cell-free protein synthesis / Plasmid: P060710-08 / References: UniProt: P12023, UniProt: Q9DBR4

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY

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Sample preparation

DetailsContents: 1.00mM chimera sample U-15N, 13C; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 296 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.5Brukercollection
NMRPipe20031121Delaglio, F.processing
NMRView5.0.4Johnson, B.A.data analysis
KUJIRA0.982Kobayashi, N.data analysis
CYANA2.0.17Guntert, P.structure solution
CYANA2.0.17Guntert, P.refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations, target function
Conformers calculated total number: 100 / Conformers submitted total number: 20

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