SASBDB entries for UniProt ID: O60828

SASDED2 – Polyglutamine tract-binding protein 1 (PQBP-1)

UniProt ID: O60828 (1-265) Polyglutamine-binding protein 1

Polyglutamine-binding protein 1 experimental SAS data
Polyglutamine tract-binding protein 1 (PQBP-1) Rg histogram
Sample: Polyglutamine-binding protein 1 monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1mM DTT,, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III on 2009 Nov 18
Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. Biophys J 102(7):1608-16 (2012)
Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 51 nm3

SASDET6 – Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7)

UniProt ID: O60828 (1-192) Polyglutamine-binding protein 1 p.Lys192Serfs*7

Polyglutamine-binding protein 1 p.Lys192Serfs*7 experimental SAS data
Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Lys192Serfs*7 dimer, 47 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 114 nm3

SASDEU6 – Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41)

UniProt ID: O60828 (1-154) Polyglutamine-binding protein 1 p.Arg153Serfs*41

Polyglutamine-binding protein 1 p.Arg153Serfs*41 experimental SAS data
Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Arg153Serfs*41 dimer, 44 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW
RgGuinier 3.6 nm
Dmax 13.0 nm
VolumePorod 100 nm3