The C-terminal region of the human p23 chaperone modulates its structure and function.

Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
Arch Biochem Biophys 565:57-67 (2015 Jan 1)

PMID: 25447839 doi: 10.1016/j.abb.2014.10.015

Submitted to SASBDB: 2016 Sep 13 Published in SASBDB: 2016 Oct 5

SASDBH6 – Full-length human p23 (1-160) Sample: Prostaglandin E synthase 3 monomer, 19 kDa Homo sapiens protein Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5 Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22 RgGuinier 2.5 nm Dmax 10.0 nm VolumePorod 40 nm3

SASDBJ6 – Truncated construct of human p23 (1-142) Sample: Prostaglandin E synthase 3 (1-142) monomer, 17 kDa Homo sapiens protein Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5 Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22 RgGuinier 2.1 nm Dmax 8.5 nm VolumePorod 36 nm3

SASDBL6 – Truncated construct of human p23 (1-117) Sample: Prostaglandin E synthase 3 (1-117) monomer, 14 kDa Homo sapiens protein Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5 Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21 RgGuinier 1.9 nm Dmax 7.0 nm VolumePorod 29 nm3

SASDBK6 – Truncated construct of human p23 (1-131) Sample: Prostaglandin E synthase 3 (1-131) monomer, 16 kDa Homo sapiens protein Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5 Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21 RgGuinier 1.9 nm Dmax 7.0 nm VolumePorod 31 nm3