| http://purl.uniprot.org/citations/19237748 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19237748 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19237748 | http://www.w3.org/2000/01/rdf-schema#comment | "3(17)alpha-Hydroxysteroid dehydrogenase (AKR1C21) is a unique member of the aldo-keto reductase (AKR) superfamily owing to its ability to reduce 17-ketosteroids to 17alpha-hydroxysteroids, as opposed to other members of the AKR family, which can only produce 17beta-hydroxysteroids. In this paper, the crystal structure of a double mutant (G225P/G226P) of AKR1C21 in complex with the coenzyme NADP(+) and the inhibitor hexoestrol refined at 2.1 A resolution is presented. Kinetic analysis and molecular-modelling studies of 17alpha- and 17beta-hydroxysteroid substrates in the active site of AKR1C21 suggested that Gly225 and Gly226 play an important role in determining the substrate stereospecificity of the enzyme. Additionally, the G225P/G226P mutation of the enzyme reduced the affinity (K(m)) for both 3alpha- and 17alpha-hydroxysteroid substrates by up to 160-fold, indicating that these residues are critical for the binding of substrates."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444908044028"xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444908044028"xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Endo S."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Endo S."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Hara A."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Hara A."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Dhagat U."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Dhagat U."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "El-Kabbani O."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "El-Kabbani O."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Mamiya H."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/author | "Mamiya H."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/name | "Acta Crystallogr. D"xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/name | "Acta Crystallogr. D"xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/pages | "257-265"xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/pages | "257-265"xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/title | "Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/title | "Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate."xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/volume | "65"xsd:string |
| http://purl.uniprot.org/citations/19237748 | http://purl.uniprot.org/core/volume | "65"xsd:string |