Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.

Necasová I, Janoušková E, Klumpler T, Hofr C, Nucleic Acids Res 45(21):12170-12180 (2017) Europe PMC

SASDB79 – Basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with telomeric DNA duplex

Basic domain of telomeric repeat-binding factor 2
telomere DNA duplex
MWexperimental 15 kDa
MWexpected 15 kDa
VPorod 20 nm3
log I(s) 2.20×10-1 2.20×10-2 2.20×10-3 2.20×10-4
Basic domain of telomeric repeat-binding factor 2 telomere DNA duplex small angle scattering data  s, nm-1
ln I(s)
Basic domain of telomeric repeat-binding factor 2 telomere DNA duplex Guinier plot ln 2.20×10-1 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Basic domain of telomeric repeat-binding factor 2 telomere DNA duplex Kratky plot 1.104 0 √3 sRg
p(r)
Basic domain of telomeric repeat-binding factor 2 telomere DNA duplex pair distance distribution function Rg: 1.8 nm 0 Dmax: 6.0 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Basic domain of telomeric repeat-binding factor 2 telomere DNA duplex MONSA model
log I(s)
 s, nm-1
SAXS data from solutions of the basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with a telomeric DNA duplex in 20 mM Tris-HCl, 50 mM LiCl, pH 7.5 were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4πsinθ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 2.9 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.

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).

Basic domain of telomeric repeat-binding factor 2 (TRF2)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   4.6 kDa
 
UniProt   Q15554 (42-86)
Sequence   FASTA
 
telomere DNA duplex
Mol. type   DNA
Olig. state   Monomer
Mon. MW   10.5 kDa
Sequence   FASTA