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- SASDB79: Basic domain of human telomeric repeat-binding factor 2 (TRF2) in... -

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Basic information

Entry
Database: SASBDB / ID: SASDB79
SampleBasic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with telomeric DNA duplex
  • Basic domain of telomeric repeat-binding factor 2 (protein), TRF2, Homo sapiens
  • telomere DNA duplex (DNA)
Function / homology
Function and homology information


axonal transport of messenger ribonucleoprotein complex / negative regulation of beta-galactosidase activity / negative regulation of telomere single strand break repair / negative regulation of telomere maintenance via recombination / telomeric loop formation / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / negative regulation of telomere capping / protection from non-homologous end joining at telomere ...axonal transport of messenger ribonucleoprotein complex / negative regulation of beta-galactosidase activity / negative regulation of telomere single strand break repair / negative regulation of telomere maintenance via recombination / telomeric loop formation / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / negative regulation of telomere capping / protection from non-homologous end joining at telomere / RNA-templated DNA biosynthetic process / negative regulation of t-circle formation / telomeric D-loop disassembly / shelterin complex / Telomere C-strand synthesis initiation / double-stranded telomeric DNA binding / regulation of telomere maintenance via telomerase / telomere capping / Telomere C-strand (Lagging Strand) Synthesis / positive regulation of telomere maintenance / nuclear telomere cap complex / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / anterograde axonal transport / Removal of the Flap Intermediate from the C-strand / G-rich strand telomeric DNA binding / regulation of telomere maintenance / protein localization to chromosome, telomeric region / negative regulation of telomere maintenance via telomere lengthening / telomeric DNA binding / negative regulation of cellular senescence / negative regulation of telomere maintenance via telomerase / Telomere Extension By Telomerase / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / axon cytoplasm / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / telomere maintenance / Meiotic synapsis / positive regulation of nitric-oxide synthase activity / male germ cell nucleus / DNA Damage/Telomere Stress Induced Senescence / cellular senescence / in utero embryonic development / chromosome, telomeric region / nuclear body / negative regulation of gene expression / protein-containing complex binding / positive regulation of gene expression / enzyme binding / protein homodimerization activity / nucleoplasm / nucleus
Similarity search - Function
Telomeric repeat-binding factor 2, Rap1-binding domain / Telomeric repeat-binding factor 2 Rap1-binding motif / Telomeric repeat-binding factor 2 / Telomeric repeat-binding factor 1/2 / Telomere repeat-binding factor, dimerisation domain superfamily / Telomere repeat-binding factor, dimerisation domain / Telomere repeat binding factor (TRF) / Myb-type HTH DNA-binding domain profile. / Myb domain / Myb-like DNA-binding domain ...Telomeric repeat-binding factor 2, Rap1-binding domain / Telomeric repeat-binding factor 2 Rap1-binding motif / Telomeric repeat-binding factor 2 / Telomeric repeat-binding factor 1/2 / Telomere repeat-binding factor, dimerisation domain superfamily / Telomere repeat-binding factor, dimerisation domain / Telomere repeat binding factor (TRF) / Myb-type HTH DNA-binding domain profile. / Myb domain / Myb-like DNA-binding domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / Homeobox-like domain superfamily
Similarity search - Domain/homology
Telomeric repeat-binding factor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationDate: 2017 Sep 13
Title: Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it
Authors: Nečasová I / Janoušková E / Klumpler T
Contact author
  • Tomas Klumpler (CEITEC - Central European Institute of Technology, Masaryk University)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #1155
Type: dummy / Radius of dummy atoms: 2.25 A / Chi-square value: 1.061 / P-value: 0.955000
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with telomeric DNA duplex
Specimen concentration: 2.9 mg/ml / Entity id: 569 / 570
BufferName: 20 mM Tris-HCl, 50 mM LiCl / pH: 7.5
Entity #569Name: TRF2 / Type: protein
Description: Basic domain of telomeric repeat-binding factor 2
Formula weight: 4.587 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q15554
Sequence:
GPPGSMAGGG GSSDGSGRAA GRRASRSSGR ARRGRHEPGL GGPAERGAG
Entity #570Type: DNA / Description: telomere DNA duplex / Formula weight: 10.522 / Num. of mol.: 1
Sequence:
GTTAGGGTTA GGGTTAGCAA TCCCAATCCC AATC

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Experimental information

BeamInstrument name: CEITEC Rigaku BioSAXS-1000 / City: Brno / : Czech Republic / Type of source: X-ray in house / Wavelength: 0.154 Å / Dist. spec. to detc.: 0.4791 mm
DetectorName: Pilatus 100K / Pixsize x: 172 mm
Scan
Title: Basic domain of human telomeric repeat-binding fac / Measurement date: May 3, 2016 / Storage temperature: 4 °C / Cell temperature: 4 °C / Exposure time: 3600 sec. / Number of frames: 6 / Unit: 1/A /
MinMax
Q0.0311 0.3004
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 184 /
MinMax
Q0.0368444 0.300399
P(R) point1 184
R0 59.46
Result
Type of curve: single_conc
Comments: The two-phase bead model of the protein-DNA complex was generated using MONSA refinement from SAXS data measured from the complex (top data-model fit) in parallel with data measured from ...Comments: The two-phase bead model of the protein-DNA complex was generated using MONSA refinement from SAXS data measured from the complex (top data-model fit) in parallel with data measured from the isolated telomeric DNA duplex (bottom data-model fit; refer to SASBDB entry SASDB89).
ExperimentalPorod
MW15.1 kDa-
Volume-20.3 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I00.2278 0.001668 0.22 0.0018
Radius of gyration, Rg1.776 nm0.017 1.711 nm0.058

MinMax
D-5.95
Guinier point5 32

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