| pubmed-article:17909281 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17909281 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:17909281 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:17909281 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:17909281 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:17909281 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17909281 | lifeskim:mentions | umls-concept:C0525733 | lld:lifeskim |
| pubmed-article:17909281 | pubmed:issue | Pt 10 | lld:pubmed |
| pubmed-article:17909281 | pubmed:dateCreated | 2007-10-2 | lld:pubmed |
| pubmed-article:17909281 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17909281 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17909281 | pubmed:abstractText | Mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) is a bifunctional enzyme that catalyses the oxidoreduction of the 3- and 17-hydroxy/keto groups of steroid substrates such as oestrogens, androgens and neurosteroids. The structure of the AKR1C21-NADPH binary complex was determined from an orthorhombic crystal belonging to space group P2(1)2(1)2(1) at a resolution of 1.8 A. In order to identify the factors responsible for the bifunctionality of AKR1C21, three steroid substrates including a 17-keto steroid, a 3-keto steroid and a 3alpha-hydroxysteroid were docked into the substrate-binding cavity. Models of the enzyme-coenzyme-substrate complexes suggest that Lys31, Gly225 and Gly226 are important for ligand recognition and orientation in the active site. | lld:pubmed |
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| pubmed-article:17909281 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17909281 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17909281 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17909281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17909281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17909281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17909281 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17909281 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17909281 | pubmed:issn | 1744-3091 | lld:pubmed |
| pubmed-article:17909281 | pubmed:author | pubmed-author:El-KabbaniOss... | lld:pubmed |
| pubmed-article:17909281 | pubmed:author | pubmed-author:HaraAkiraA | lld:pubmed |
| pubmed-article:17909281 | pubmed:author | pubmed-author:CarboneVincen... | lld:pubmed |
| pubmed-article:17909281 | pubmed:author | pubmed-author:EndoSatoshiS | lld:pubmed |
| pubmed-article:17909281 | pubmed:author | pubmed-author:Schulze-Bries... | lld:pubmed |
| pubmed-article:17909281 | pubmed:author | pubmed-author:ChungRoland... | lld:pubmed |
| pubmed-article:17909281 | pubmed:author | pubmed-author:DhagatUrmiU | lld:pubmed |
| pubmed-article:17909281 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17909281 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17909281 | pubmed:volume | 63 | lld:pubmed |
| pubmed-article:17909281 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17909281 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17909281 | pubmed:pagination | 825-30 | lld:pubmed |
| pubmed-article:17909281 | pubmed:dateRevised | 2010-9-15 | lld:pubmed |
| pubmed-article:17909281 | pubmed:meshHeading | pubmed-meshheading:17909281... | lld:pubmed |
| pubmed-article:17909281 | pubmed:meshHeading | pubmed-meshheading:17909281... | lld:pubmed |
| pubmed-article:17909281 | pubmed:meshHeading | pubmed-meshheading:17909281... | lld:pubmed |
| pubmed-article:17909281 | pubmed:meshHeading | pubmed-meshheading:17909281... | lld:pubmed |
| pubmed-article:17909281 | pubmed:meshHeading | pubmed-meshheading:17909281... | lld:pubmed |
| pubmed-article:17909281 | pubmed:meshHeading | pubmed-meshheading:17909281... | lld:pubmed |
| pubmed-article:17909281 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17909281 | pubmed:articleTitle | Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme. | lld:pubmed |
| pubmed-article:17909281 | pubmed:affiliation | Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Victoria 3052, Australia. | lld:pubmed |
| pubmed-article:17909281 | pubmed:publicationType | Journal Article | lld:pubmed |
