| General information | | DisProt: | DP00358 | | Name: | Prostaglandin E synthase 3 | | Synonym(s): | TEBP_HUMAN
Prostaglandin E synthase 3
EC=5.3.99.3
Cytosolic prostaglandin E2 synthase
cPGES
Telomerase-binding protein p23
Hsp90 co-chaperone
Progesterone receptor complex p23
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q15185 | | UniGene: | Hs.50425 | | SwissProt: | TEBP_HUMAN | | TrEMBL: | | | NCBI (GI): | 8928247 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 160 | | Percent disordered: | 28% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID - 60
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF - 120
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
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| Functional narrative |
p23 is a co-chaperone of the heat shock protein Hsp90. p23 binds to Hsp90 in its ATP-bound state and, on its own, interacts specifically with non-native proteins. The binding site for Hsp90 is contained in the folded domain of p23 and for efficient interaction of p23 with non-native proteins both the folded domain and the C-terminal unstructured region are required. Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 131 - 160 | | Length: | 30 | | Region sequence: |
GGDEDVDLPEVDGADDDSQDSDDEKMPDLE | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via an order to disorder transition
| | Functional classes: | Chaperones
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; potassium phosphate (pH 6.8) 40 mM)
- Sensitivity to proteolysis (298 K; EDTA 5 mM; Hepes-KOH (pH 7.5) 40 mM)
| References:
- Weikl T, Abelmann K, Buchner J. "An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function." J Mol Biol. 1999; 293(3): 685-91. PubMed: 10543959
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 111 - 125 | | Length: | 15 | | Region sequence: |
DDSDEDMSNFDRFSE | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | | | Functional subclasses: | | Detection methods:
- X-ray crystallography (pH: 9; Bicine (reservoir solution) 0.1 M; (NH4)2SO4 (reservoir solution, 1.9-2.1 M); Tris-HCl (pH 7.5) 10 mM)
| References:
- Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO. "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone." J Biol Chem. 2000; 275(30): 23045-52. PubMed: 10811660
| Comments:
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| References |
- Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO. "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone." J Biol Chem. 2000; 275(30): 23045-52. PubMed: 10811660
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