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- PDB-2uwq: Solution structure of ASPP2 N-terminus -

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Basic information

Entry
Database: PDB / ID: 2uwq
TitleSolution structure of ASPP2 N-terminus
ComponentsAPOPTOSIS-STIMULATING OF P53 PROTEIN 2
KeywordsAPOPTOSIS / ASPP2 / UBIQUITIN-LIKE / SH3-DOMAIN / CELL CYCLE / ANK REPEAT / SH3-BINDING
Function / homology
Function and homology information


TP53 Regulates Transcription of Death Receptors and Ligands / Activation of PUMA and translocation to mitochondria / Regulation of TP53 Activity through Association with Co-factors / positive regulation of execution phase of apoptosis / TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain / TP53 Regulates Transcription of Genes Involved in Cytochrome C Release / intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of cell cycle / NF-kappaB binding / SH3 domain binding ...TP53 Regulates Transcription of Death Receptors and Ligands / Activation of PUMA and translocation to mitochondria / Regulation of TP53 Activity through Association with Co-factors / positive regulation of execution phase of apoptosis / TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain / TP53 Regulates Transcription of Genes Involved in Cytochrome C Release / intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of cell cycle / NF-kappaB binding / SH3 domain binding / p53 binding / cell junction / cell cycle / perinuclear region of cytoplasm / signal transduction / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
: / : / : / Apoptosis-stimulating of p53 protein 2-like, N-terminal RA domain / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / SH3 domain / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats ...: / : / : / Apoptosis-stimulating of p53 protein 2-like, N-terminal RA domain / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / SH3 domain / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Src homology 3 domains / Ubiquitin-like (UB roll) / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Ubiquitin-like domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
Apoptosis-stimulating of p53 protein 2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / simulated annealing
AuthorsTidow, H. / Rutherford, T.J. / Andreeva, A. / Fersht, A.R.
CitationJournal: J. Mol. Biol. / Year: 2007
Title: Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.
Authors: Tidow, H. / Andreeva, A. / Rutherford, T.J. / Fersht, A.R.
History
DepositionMar 22, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 10, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 9, 2018Group: Data collection / Database references / Category: citation / pdbx_nmr_spectrometer
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _pdbx_nmr_spectrometer.model
Revision 1.4May 15, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: APOPTOSIS-STIMULATING OF P53 PROTEIN 2


Theoretical massNumber of molelcules
Total (without water)9,9761
Polymers9,9761
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)20 / 90LOWEST ENERGY, NO VIOLATIONS
RepresentativeModel #19

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Components

#1: Protein APOPTOSIS-STIMULATING OF P53 PROTEIN 2 / TUMOR SUPPRESSOR P53-BINDING PROTEIN 2 / P53-BINDING PROTEIN 2 / P53BP2 / 53BP2 / BCL2-BINDING ...TUMOR SUPPRESSOR P53-BINDING PROTEIN 2 / P53-BINDING PROTEIN 2 / P53BP2 / 53BP2 / BCL2-BINDING PROTEIN / BBP / RENAL CARCINOMA ANTIGEN NY-REN-51


Mass: 9976.222 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-83
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q13625
Sequence detailsN-TERMINAL GGS DUE TO CLEAVAGE FROM FUSION PROTEIN

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111COSY
121TOCSY
131HNCO
141HN(CA)CO
151CBCA(CO)NH
161HN(CA)CB
171CC(CO)NH
281NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY.

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Sample preparation

DetailsContents: 25MM PHOSPHATE, PH7.2, 150MM NACL, 5MM DTT, 5%D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
1213 mM7.2 1.0 atm298.0 K
2213 mM7.2 1.0 atm298.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Bruker AVANCEBrukerAVANCE8002

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Processing

NMR software
NameDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARRENrefinement
CNSstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY, NO VIOLATIONS / Conformers calculated total number: 90 / Conformers submitted total number: 20

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