Three-Dimensional Structure of Rat Liver 3α-Hydroxysteroid/ Dihydrodiol Dehydrogenase: A Member of the Aldo-Keto Reductase Superfamily
The 3.0-$\overset{circ}{Mathrm A}$-resolution x-ray structure of rat liver 3α-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3α-HSD, EC 1.1.1.50) was determined by molecular replacement using human placental aldose reductase as the search model. The protein folds into an α/β or triose-phosp...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1994-03, Vol.91 (7), p.2517-2521 |
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| creator | Hoog, Susan S. Pawlowski, John E. Alzari, Pedro M. Penning, Trevor M. Lewis, Mitchell |
| description | The 3.0-$\overset{circ}{Mathrm A}$-resolution x-ray structure of rat liver 3α-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3α-HSD, EC 1.1.1.50) was determined by molecular replacement using human placental aldose reductase as the search model. The protein folds into an α/β or triose-phosphate isomerase barrel and lacks a canonical Rossmann fold for binding pyridine nucleotide. The structure contains a concentration of hydrophobic amino acids that lie in a cavity near the top of the barrel and that are presumed to be involved in binding hydrophobic substrates (steroids, prostaglandins, and polycyclic aromatic hydrocarbons) and inhibitors (nonsteroidal antiinflammatory drugs). At the distal end of this cavity lie three residues in close proximity that have been implicated in catalysis by site-directed mutagenesis-Tyr-55, Asp-50, and Lys-84. Tyr-55 is postulated to act as the general acid. 3α-HSD shares significant sequence identity with other HSDs that belong to the aido-keto reductase superfamily and these may show similar architecture. Other members of this family include prostaglandin F synthase and ρ-crystallin. By contrast, 3α-HSD shares no sequence identity with HSDs that are members of the short-chain alcohol dehydrogenase family but does contain the Tyr-Xaa-Xaa-Xaa-Lys consensus sequence implicated in catalysis in this family. In the 3α-HSD structure these residues are on the periphery of the barrel and are unlikely to participate in catalysis. |
| doi_str_mv | 10.1073/pnas.91.7.2517 |
| format | Article |
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The protein folds into an α/β or triose-phosphate isomerase barrel and lacks a canonical Rossmann fold for binding pyridine nucleotide. The structure contains a concentration of hydrophobic amino acids that lie in a cavity near the top of the barrel and that are presumed to be involved in binding hydrophobic substrates (steroids, prostaglandins, and polycyclic aromatic hydrocarbons) and inhibitors (nonsteroidal antiinflammatory drugs). At the distal end of this cavity lie three residues in close proximity that have been implicated in catalysis by site-directed mutagenesis-Tyr-55, Asp-50, and Lys-84. Tyr-55 is postulated to act as the general acid. 3α-HSD shares significant sequence identity with other HSDs that belong to the aido-keto reductase superfamily and these may show similar architecture. Other members of this family include prostaglandin F synthase and ρ-crystallin. By contrast, 3α-HSD shares no sequence identity with HSDs that are members of the short-chain alcohol dehydrogenase family but does contain the Tyr-Xaa-Xaa-Xaa-Lys consensus sequence implicated in catalysis in this family. In the 3α-HSD structure these residues are on the periphery of the barrel and are unlikely to participate in catalysis.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.91.7.2517</identifier><identifier>PMID: 8146147</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) ; 3-Hydroxysteroid Dehydrogenases ; 3-Hydroxysteroid Dehydrogenases - chemistry ; 3-Hydroxysteroid Dehydrogenases - metabolism ; Aldehyde Reductase ; Aldehyde Reductase - chemistry ; Amino acids ; Analytical, structural and metabolic biochemistry ; Animals ; Biochemistry ; Biochemistry, Molecular Biology ; Bioinformatics ; Biological and medical sciences ; Biological Physics ; Catalysis ; Cellular Biology ; Chemical Sciences ; Computer Science ; Consensus Sequence ; Cristallography ; Crystallins ; Crystallins - chemistry ; Crystallography, X-Ray ; Dehydrogenases ; Electron density ; Enzymes ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrogen bonds ; Hydroxyprostaglandin Dehydrogenases ; Hydroxyprostaglandin Dehydrogenases - chemistry ; Life Sciences ; Liver ; Models, Chemical ; Models, Molecular ; Mutagenesis, Site-Directed ; Oxidoreductases ; Physics ; Prostaglandins ; Protein Conformation ; Protein Folding ; Rats ; Steroids ; Steroids - metabolism ; Structural Biology ; Substrate Specificity</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1994-03, Vol.91 (7), p.2517-2521</ispartof><rights>Copyright 1994 The National Academy of Sciences of the United States of America</rights><rights>1994 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5057-3e352e77e7e2d5d942e9bec5f000591469ae47d31de8328b5068fcb23c0998143</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/91/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2364265$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2364265$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,309,310,314,727,780,784,789,790,803,885,23930,23931,25140,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4169676$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8146147$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://pasteur.hal.science/pasteur-03136543$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Hoog, Susan S.</creatorcontrib><creatorcontrib>Pawlowski, John E.</creatorcontrib><creatorcontrib>Alzari, Pedro M.</creatorcontrib><creatorcontrib>Penning, Trevor M.</creatorcontrib><creatorcontrib>Lewis, Mitchell</creatorcontrib><title>Three-Dimensional Structure of Rat Liver 3α-Hydroxysteroid/ Dihydrodiol Dehydrogenase: A Member of the Aldo-Keto Reductase Superfamily</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The 3.0-$\overset{circ}{Mathrm A}$-resolution x-ray structure of rat liver 3α-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3α-HSD, EC 1.1.1.50) was determined by molecular replacement using human placental aldose reductase as the search model. The protein folds into an α/β or triose-phosphate isomerase barrel and lacks a canonical Rossmann fold for binding pyridine nucleotide. The structure contains a concentration of hydrophobic amino acids that lie in a cavity near the top of the barrel and that are presumed to be involved in binding hydrophobic substrates (steroids, prostaglandins, and polycyclic aromatic hydrocarbons) and inhibitors (nonsteroidal antiinflammatory drugs). At the distal end of this cavity lie three residues in close proximity that have been implicated in catalysis by site-directed mutagenesis-Tyr-55, Asp-50, and Lys-84. Tyr-55 is postulated to act as the general acid. 3α-HSD shares significant sequence identity with other HSDs that belong to the aido-keto reductase superfamily and these may show similar architecture. Other members of this family include prostaglandin F synthase and ρ-crystallin. By contrast, 3α-HSD shares no sequence identity with HSDs that are members of the short-chain alcohol dehydrogenase family but does contain the Tyr-Xaa-Xaa-Xaa-Lys consensus sequence implicated in catalysis in this family. In the 3α-HSD structure these residues are on the periphery of the barrel and are unlikely to participate in catalysis.</description><subject>3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)</subject><subject>3-Hydroxysteroid Dehydrogenases</subject><subject>3-Hydroxysteroid Dehydrogenases - chemistry</subject><subject>3-Hydroxysteroid Dehydrogenases - metabolism</subject><subject>Aldehyde Reductase</subject><subject>Aldehyde Reductase - chemistry</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biological Physics</subject><subject>Catalysis</subject><subject>Cellular Biology</subject><subject>Chemical Sciences</subject><subject>Computer Science</subject><subject>Consensus Sequence</subject><subject>Cristallography</subject><subject>Crystallins</subject><subject>Crystallins - chemistry</subject><subject>Crystallography, X-Ray</subject><subject>Dehydrogenases</subject><subject>Electron density</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen bonds</subject><subject>Hydroxyprostaglandin Dehydrogenases</subject><subject>Hydroxyprostaglandin Dehydrogenases - chemistry</subject><subject>Life Sciences</subject><subject>Liver</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed</subject><subject>Oxidoreductases</subject><subject>Physics</subject><subject>Prostaglandins</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Rats</subject><subject>Steroids</subject><subject>Steroids - metabolism</subject><subject>Structural Biology</subject><subject>Substrate Specificity</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc1u1DAUhSMEKkNhywokLxC7pHZsxzHqZtQpDGIQUlvWlpPcNK4ycWQno84T8Dx9EZ4JhxmigljZ8vnO_fGJotcEJwQLetZ32ieSJCJJORFPogXBksQZk_hptMA4FXHOUvY8euH9HcZY8hyfRCc5YRlhYhH9uGkcQLwyW-i8sZ1u0fXgxnIYHSBboys9oI3ZgUP050O83lfO3u_9AM6a6gytTDO9VMa2aAW_77cQBoIPaIm-wrYIvlBkaAAt28rGX2Cw6AqqUD9A6HrswdV6a9r9y-hZrVsPr47nafT94-XNxTrefPv0-WK5iUuOuYgpUJ6CECAgrXglWQqygJLXYTUuw1JSAxMVJRXkNM0LjrO8LouUlljKsDQ9jc4Pdfux2EJVQjc43arema12e2W1UX8rnWnUrd0pRhnGwR4f7M0_pvVyo3odPmZ0ClNCM87ojgQ-OfCls947qGcTwWrKT035KUmUUFN-wfD28Xwzfgws6O-Ouvalbmunu9L4GWMkk5nIAvb-iE3l_6hzG1WPbTvA_fCo33_BoL856Hd-sG4GUpqxNOP0Fx8Sxxg</recordid><startdate>19940329</startdate><enddate>19940329</enddate><creator>Hoog, Susan S.</creator><creator>Pawlowski, John E.</creator><creator>Alzari, Pedro M.</creator><creator>Penning, Trevor M.</creator><creator>Lewis, Mitchell</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope><scope>5PM</scope></search><sort><creationdate>19940329</creationdate><title>Three-Dimensional Structure of Rat Liver 3α-Hydroxysteroid/ Dihydrodiol Dehydrogenase: A Member of the Aldo-Keto Reductase Superfamily</title><author>Hoog, Susan S. ; Pawlowski, John E. ; Alzari, Pedro M. ; Penning, Trevor M. ; Lewis, Mitchell</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5057-3e352e77e7e2d5d942e9bec5f000591469ae47d31de8328b5068fcb23c0998143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)</topic><topic>3-Hydroxysteroid Dehydrogenases</topic><topic>3-Hydroxysteroid Dehydrogenases - chemistry</topic><topic>3-Hydroxysteroid Dehydrogenases - metabolism</topic><topic>Aldehyde Reductase</topic><topic>Aldehyde Reductase - chemistry</topic><topic>Amino acids</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biological Physics</topic><topic>Catalysis</topic><topic>Cellular Biology</topic><topic>Chemical Sciences</topic><topic>Computer Science</topic><topic>Consensus Sequence</topic><topic>Cristallography</topic><topic>Crystallins</topic><topic>Crystallins - chemistry</topic><topic>Crystallography, X-Ray</topic><topic>Dehydrogenases</topic><topic>Electron density</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen bonds</topic><topic>Hydroxyprostaglandin Dehydrogenases</topic><topic>Hydroxyprostaglandin Dehydrogenases - chemistry</topic><topic>Life Sciences</topic><topic>Liver</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Mutagenesis, Site-Directed</topic><topic>Oxidoreductases</topic><topic>Physics</topic><topic>Prostaglandins</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Rats</topic><topic>Steroids</topic><topic>Steroids - metabolism</topic><topic>Structural Biology</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hoog, Susan S.</creatorcontrib><creatorcontrib>Pawlowski, John E.</creatorcontrib><creatorcontrib>Alzari, Pedro M.</creatorcontrib><creatorcontrib>Penning, Trevor M.</creatorcontrib><creatorcontrib>Lewis, Mitchell</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hoog, Susan S.</au><au>Pawlowski, John E.</au><au>Alzari, Pedro M.</au><au>Penning, Trevor M.</au><au>Lewis, Mitchell</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-Dimensional Structure of Rat Liver 3α-Hydroxysteroid/ Dihydrodiol Dehydrogenase: A Member of the Aldo-Keto Reductase Superfamily</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1994-03-29</date><risdate>1994</risdate><volume>91</volume><issue>7</issue><spage>2517</spage><epage>2521</epage><pages>2517-2521</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>The 3.0-$\overset{circ}{Mathrm A}$-resolution x-ray structure of rat liver 3α-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3α-HSD, EC 1.1.1.50) was determined by molecular replacement using human placental aldose reductase as the search model. The protein folds into an α/β or triose-phosphate isomerase barrel and lacks a canonical Rossmann fold for binding pyridine nucleotide. The structure contains a concentration of hydrophobic amino acids that lie in a cavity near the top of the barrel and that are presumed to be involved in binding hydrophobic substrates (steroids, prostaglandins, and polycyclic aromatic hydrocarbons) and inhibitors (nonsteroidal antiinflammatory drugs). At the distal end of this cavity lie three residues in close proximity that have been implicated in catalysis by site-directed mutagenesis-Tyr-55, Asp-50, and Lys-84. Tyr-55 is postulated to act as the general acid. 3α-HSD shares significant sequence identity with other HSDs that belong to the aido-keto reductase superfamily and these may show similar architecture. Other members of this family include prostaglandin F synthase and ρ-crystallin. By contrast, 3α-HSD shares no sequence identity with HSDs that are members of the short-chain alcohol dehydrogenase family but does contain the Tyr-Xaa-Xaa-Xaa-Lys consensus sequence implicated in catalysis in this family. In the 3α-HSD structure these residues are on the periphery of the barrel and are unlikely to participate in catalysis.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8146147</pmid><doi>10.1073/pnas.91.7.2517</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1994-03, Vol.91 (7), p.2517-2521 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_91_7_2517_fulltext |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) 3-Hydroxysteroid Dehydrogenases 3-Hydroxysteroid Dehydrogenases - chemistry 3-Hydroxysteroid Dehydrogenases - metabolism Aldehyde Reductase Aldehyde Reductase - chemistry Amino acids Analytical, structural and metabolic biochemistry Animals Biochemistry Biochemistry, Molecular Biology Bioinformatics Biological and medical sciences Biological Physics Catalysis Cellular Biology Chemical Sciences Computer Science Consensus Sequence Cristallography Crystallins Crystallins - chemistry Crystallography, X-Ray Dehydrogenases Electron density Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen bonds Hydroxyprostaglandin Dehydrogenases Hydroxyprostaglandin Dehydrogenases - chemistry Life Sciences Liver Models, Chemical Models, Molecular Mutagenesis, Site-Directed Oxidoreductases Physics Prostaglandins Protein Conformation Protein Folding Rats Steroids Steroids - metabolism Structural Biology Substrate Specificity |
| title | Three-Dimensional Structure of Rat Liver 3α-Hydroxysteroid/ Dihydrodiol Dehydrogenase: A Member of the Aldo-Keto Reductase Superfamily |
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