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Yorodumi- SASDB79: Basic domain of human telomeric repeat-binding factor 2 (TRF2) in... -
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-Basic information
Entry | Database: SASBDB / ID: SASDB79 |
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Sample | Basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with telomeric DNA duplex
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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 |
Biological species | Homo sapiens (human) |
Citation | Date: 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDB79 |
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-Related structure data
Related structure data | C: citing same article (ref.) |
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Similar structure data |
-External links
Related items in Molecule of the Month |
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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
Sample | Name: 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 |
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Buffer | Name: 20 mM Tris-HCl, 50 mM LiCl / pH: 7.5 |
Entity #569 | Name: 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 #570 | Type: DNA / Description: telomere DNA duplex / Formula weight: 10.522 / Num. of mol.: 1 Sequence: GTTAGGGTTA GGGTTAGCAA TCCCAATCCC AATC |
-Experimental information
Beam | Instrument name: CEITEC Rigaku BioSAXS-1000 / City: Brno / 国: Czech Republic / Type of source: X-ray in house / Wavelength: 0.154 Å / Dist. spec. to detc.: 0.4791 mm | |||||||||||||||||||||||||||||||||
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Detector | Name: 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 /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 184 /
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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).
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