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Yorodumi- SASDBL6: Truncated construct of human p23 (1-117) (Prostaglandin E synthas... -
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-Basic information
Entry | Database: SASBDB / ID: SASDBL6 |
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Sample | Truncated construct of human p23 (1-117)
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Function / homology | Function and homology information lung saccule development / prostaglandin-E synthase / prostaglandin-E synthase activity / telomerase activity / intracellular glucocorticoid receptor signaling pathway / Aryl hydrocarbon receptor signalling / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / cyclooxygenase pathway / telomerase holoenzyme complex / glycogen biosynthetic process ...lung saccule development / prostaglandin-E synthase / prostaglandin-E synthase activity / telomerase activity / intracellular glucocorticoid receptor signaling pathway / Aryl hydrocarbon receptor signalling / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / cyclooxygenase pathway / telomerase holoenzyme complex / glycogen biosynthetic process / protein folding chaperone complex / prostaglandin biosynthetic process / skin development / telomerase holoenzyme complex assembly / chaperone cofactor-dependent protein refolding / telomere maintenance via telomerase / HSF1 activation / chaperone-mediated protein complex assembly / Attenuation phase / DNA polymerase binding / positive regulation of phosphorylation / positive regulation of telomerase activity / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / telomere maintenance / ESR-mediated signaling / Hsp90 protein binding / unfolded protein binding / protein folding / fibroblast proliferation / protein-folding chaperone binding / Estrogen-dependent gene expression / Potential therapeutics for SARS / chromosome, telomeric region / protein stabilization / signal transduction / protein-containing complex / nucleoplasm / nucleus / cytosol Similarity search - Function |
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, ...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 |
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-Structure visualization
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-Data source
SASBDB page | SASDBL6 |
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-Related structure data
Related structure data | C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-External links
Related items in Molecule of the Month |
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-Models
-Sample
Sample | Name: Truncated construct of human p23 (1-117) / Specimen concentration: 1.00-2.00 |
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Buffer | Name: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol / pH: 7.5 |
Entity #407 | Name: PTGES, Sba1, p23 / Type: protein / Description: Prostaglandin E synthase 3 (1-117) / Formula weight: 14.031 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q15185 Sequence: GSMQPASAKW YDRRDYVFIE FCVEDSKDVN VNFEKSKLTF SCLGGSDNFK HLNEIDLFHC IDPNDSKHKR TDRSILCCLR KGESGQSWPR LTKERAKLNW LSVDFNNWKD WEDDSDEDM |
-Experimental information
Beam | Instrument name: Brazilian Synchrotron Light Laboratory SAXS1 Beamline City: Campinas / 国: Brazil / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.1488 Å / Dist. spec. to detc.: 1 mm | |||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 300K / Type: 20Hz | |||||||||||||||||||||||||||||||||
Scan | Title: Truncated construct of human p23 (1-117) / Measurement date: Jun 21, 2013 / Storage temperature: 4 °C / Cell temperature: 20 °C / Exposure time: 30 sec. / Number of frames: 2 / Unit: 1/A /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 278 /
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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 ...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.
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