SASDBH6: Full-length human p23 (1-160) (Prostaglandin E synthase 3, PTGES,...

Basic information

Entry

Database: SASBDB / ID: SASDBH6

Sample

Full-length human p23 (1-160)

• Prostaglandin E synthase 3 (protein), PTGES, Sba1, p23, Homo sapiens

Function / homology

Function:

lung saccule development / prostaglandin-E synthase / prostaglandin-E synthase activity / nuclear receptor-mediated glucocorticoid signaling pathway / prostanoid biosynthetic process / Aryl hydrocarbon receptor signalling / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / glycogen biosynthetic process / telomerase holoenzyme complex / protein folding chaperone complex / prostaglandin biosynthetic process / skin development / telomerase holoenzyme complex assembly / : / HSF1 activation / telomere maintenance via telomerase / Attenuation phase / chaperone-mediated protein complex assembly / DNA polymerase binding / positive regulation of telomere maintenance via telomerase / telomere maintenance / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / ESR-mediated signaling / Hsp90 protein binding / telomerase activity / unfolded protein binding / protein folding / protein-folding chaperone binding / fibroblast proliferation / Estrogen-dependent gene expression / Potential therapeutics for SARS / chromosome, telomeric region / protein stabilization / signal transduction / protein-containing complex / nucleoplasm / nucleus / cytosol

Domain/homology:

Co-chaperone protein p23-like / CS domain / CS domain / CS domain profile. / HSP20-like chaperone

Component:

Prostaglandin E synthase 3

• Biological species: Homo sapiens (human)
• Citation: Journal: Arch Biochem Biophys / Year: 2015; Title: The C-terminal region of the human p23 chaperone modulates its structure and function.; Authors: Thiago V Seraphim / Lisandra M Gava / David Z Mokry / Thiago C Cagliari / Leandro R S Barbosa / Carlos H I Ramos / Júlio C Borges / ; Abstract: The p23 protein is a chaperone widely involved in protein homeostasis, well known as an Hsp90 co-chaperone since it also controls the Hsp90 chaperone cycle. Human p23 includes a β-sheet domain, responsible for interacting with Hsp90; and a charged C-terminal region whose function is not clear, but seems to be natively unfolded. p23 can undergo caspase-dependent proteolytic cleavage to form p19 (p231-142), which is involved in apoptosis, while p23 has anti-apoptotic activity. To better elucidate the function of the human p23 C-terminal region, we studied comparatively the full-length human p23 and three C-terminal truncation mutants: p23₁₋₁₁₇; p23₁₋₁₃₁ and p23₁₋₁₄₂. Our data indicate that p23 and p19 have distinct characteristics, whereas the other two truncations behave similarly, with some differences to p23 and p19. We found that part of the C-terminal region can fold in an α-helix conformation and slightly contributes to p23 thermal-stability, suggesting that the C-terminal interacts with the β-sheet domain. As a whole, our results suggest that the C-terminal region of p23 is critical for its structure-function relationship. A mechanism where the human p23 C-terminal region behaves as an activation/inhibition module for different p23 activities is proposed.

Contact author

• Júlio Borges (Instituto de Química de São Carlos, São Carlos - SP - Brasil)

Models

Sample

• Sample: Name: Full-length human p23 (1-160) / Specimen concentration: 1.00-2.00
• Buffer: Name: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol / pH: 7.5

Entity #404

Name: PTGES, Sba1, p23 / Type: protein / Description: Prostaglandin E synthase 3 / Formula weight: 18.841 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q15185
Sequence:

GSMQPASAKW YDRRDYVFIE FCVEDSKDVN VNFEKSKLTF SCLGGSDNFK HLNEIDLFHC IDPNDSKHKR TDRSILCCLR KGESGQSWPR LTKERAKLNW LSVDFNNWKD WEDDSDEDMS NFDRFSEMMN NMGGDEDVDL PEVDGADDDS QDSDDEKMPD LE

Experimental information

• Beam: Instrument name: Brazilian Synchrotron Light Laboratory SAXS1 Beamline; City: Campinas / 国: Brazil / Type of source: X-ray synchrotron / Wavelength: 0.1488 Å / Dist. spec. to detc.: 1 mm
• Detector: Name: Pilatus 300K / Type: 20Hz

Scan

Title: Full-length human p23 (1-160) / Measurement date: Jun 22, 2012 / Storage temperature: 4 °C / Cell temperature: 20 °C / Exposure time: 30 sec. / Number of frames: 2 / Unit: 1/A /

	Min	Max
Q	0.0206	0.3684

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 278 /

	Min	Max
Q	0.02059	0.3684
P(R) point	1	278
R	0	100

Result

Type of curve: single_conc
Comments: Samples were measured at 1 mg/mL and 2 mg/mL in 1 mm path-length mica cells. All curves were inspected for X-ray damage and aggregation. The experimental molecular weight was determined by analytical ultracentrifugation.

	Experimental	Porod
MW	21 kDa	-
Volume	-	40 nm3

	P(R) error	Guinier	Guinier error	P(R)
Forward scattering, I0	4.0E-5	0.019	6.0E-5	-
Radius of gyration, Rg	0.01	2.53 nm	0.12	2.69 nm

	Min	Max
D	-	10
Guinier point	3	26