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

SASDC62 – Basic domain of telomeric repeat-binding factor 2 (TRF2)

Basic domain of telomeric repeat-binding factor 2
MWexperimental 5 kDa
MWexpected 5 kDa
VPorod 4 nm3
log I(s) 1.03×10-1 1.03×10-2 1.03×10-3 1.03×10-4
Basic domain of telomeric repeat-binding factor 2 small angle scattering data  s, nm-1
ln I(s)
Basic domain of telomeric repeat-binding factor 2 Guinier plot ln 1.03×10-1 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Basic domain of telomeric repeat-binding factor 2 Kratky plot 1.104 0 √3 sRg
p(r)
Basic domain of telomeric repeat-binding factor 2 pair distance distribution function Rg: 1.8 nm 0 Dmax: 7.1 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of the basic domain of telomeric repeat-binding factor 2 (TRF2) in 50 mM sodium phosphate, 50 mM NaCl, pH 7, 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 = 4π sin θ/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 1.2 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.

Tags: idp
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