Linked Life Data

12037313

Source:http://linkedlifedata.com/resource/pubmed/id/12037313

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6 Pt 2
pubmed:dateCreated
2002-5-30
pubmed:abstractText
17beta-Hydroxysteroid dehydrogenases (17beta-HSDs) catalyze the last step in the biosynthesis of all androgens and estrogens, thus playing a pivotal role in sex-hormone metabolism. Human 17beta-HSD type 5 (17beta-HSD5) catalyzes hydride transfer at the 17beta-hydroxy position, but possesses high sequence homology to 3alpha-hydroxysteroid dehydrogenases (3alpha-HSD). Two crystal forms of 17beta-HSD5 in an enzyme-testosterone-NADP ternary complex have been obtained under different crystallization conditions. A form I crystal obtained at pH 8.5 diffracted to 1.32 A. It belonged to space group P2(1), with unit-cell parameters a = 47.41, b = 77.16, c = 48.67 A, beta = 116.32 degrees. Form II crystals obtained at pH 6.5 diffracted to 2.0 A and belonged to space group P6(3), with unit-cell parameters a = b = 110.58, c = 56.89 A.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1048-50
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Purification, crystallization and preliminary X-ray diffraction results of human 17beta-hydroxysteroid dehydrogenase type 5.
pubmed:affiliation
Molecular Endocrinology Laboratory, CHUL Research Center, Laval University, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't