4xo7 - Revision history

OCA at 13:01, 1 March 2024

2024-03-01T13:01:23Z

←Older revision		Revision as of 13:01, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4xo7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XO7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4xo7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XO7 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.75Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo7 OCA], [https://pdbe.org/4xo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xo7 RCSB], [https://www.ebi.ac.uk/pdbsum/4xo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xo7 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo7 OCA], [https://pdbe.org/4xo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xo7 RCSB], [https://www.ebi.ac.uk/pdbsum/4xo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xo7 ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN] Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.<ref>PMID:8573067</ref>		[https://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN] Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.<ref>PMID:8573067</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human 3alpha-HSD3 (3alpha-hydroxysteroid dehydrogenase type 3) plays an essential role in the inactivation of the most potent androgen 5alpha-DHT (5alpha-dihydrotestosterone). The present study attempts to obtain the important structure of 3alpha-HSD3 in complex with 5alpha-DHT and to investigate the role of 3alpha-HSD3 in breast cancer cells. We report the crystal structure of human 3alpha-HSD3.NADP(+).A-dione (5alpha-androstane-3,17-dione)/epi-ADT (epiandrosterone) complex, which was obtained by co-crystallization with 5alpha-DHT in the presence of NADP(+) Although 5alpha-DHT was introduced during the crystallization, oxidoreduction of 5alpha-DHT occurred. The locations of A-dione and epi-ADT were identified in the steroid-binding sites of two 3alpha-HSD3 molecules per crystal asymmetric unit. An overlay showed that A-dione and epi-ADT were oriented upside-down and flipped relative to each other, providing structural clues for 5alpha-DHT reverse binding in the enzyme with the generation of different products. Moreover, we report the crystal structure of the 3alpha-HSD3.NADP(+).4-dione (4-androstene-3,17-dione) complex. When a specific siRNA (100 nM) was used to suppress 3alpha-HSD3 expression without interfering with 3alpha-HSD4, which shares a highly homologous active site, the 5alpha-DHT concentration increased, whereas MCF7 cell growth was suppressed. The present study provides structural clues for 5alpha-DHT reverse binding within 3alpha-HSD3, and demonstrates for the first time that down-regulation of 3alpha-HSD3 decreases MCF7 breast cancer cell growth.
-
-	Human 3alpha-hydroxysteroid dehydrogenase type 3: structural clues of 5alpha-DHT reverse binding and enzyme down-regulation decreasing MCF7 cell growth.,Zhang B, Hu XJ, Wang XQ, Theriault JF, Zhu DW, Shang P, Labrie F, Lin SX Biochem J. 2016 Apr 15;473(8):1037-46. doi: 10.1042/BCJ20160083. Epub 2016 Feb, 29. PMID:26929402<ref>PMID:26929402</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4xo7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:45, 26 April 2023

2023-04-26T17:45:23Z

←Older revision		Revision as of 17:45, 26 April 2023
Line 1:		Line 1:

	==Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one==		==Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one==
-	<StructureSection load='4xo7' size='340' side='right' caption='[[4xo7]], [[Resolution\|resolution]] 1.75Å' scene=''>	+	<StructureSection load='4xo7' size='340' side='right'caption='[[4xo7]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4xo7]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4XO7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4xo7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XO7 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l1w\|4l1w]], [[4nnf\|4nnf]], [[4xo6\|4xo6]]</td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo7 OCA], [https://pdbe.org/4xo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xo7 RCSB], [https://www.ebi.ac.uk/pdbsum/4xo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xo7 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AKR1C2, DDH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo7 OCA], [~~http~~://pdbe.org/4xo7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4xo7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4xo7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4xo7 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN]] Defects in AKR1C2 are a cause of 46,XY sex reversal type 8 (SRXY8) [MIM:[~~http~~://omim.org/entry/614279 614279]]. A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.<ref>PMID:21802064</ref>	+	[https://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN] Defects in AKR1C2 are a cause of 46,XY sex reversal type 8 (SRXY8) [MIM:[https://omim.org/entry/614279 614279]. A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.<ref>PMID:21802064</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN]] Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.<ref>PMID:8573067</ref>	+	[https://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN] Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.<ref>PMID:8573067</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4xo7" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4xo7" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Hydroxysteroid dehydrogenase 3D structures\|Hydroxysteroid dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Hu, X J~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Lin, S~~ X]]	+	[[Category: Hu X-J]]
-	~~[[Category: Zhang, B]]~~	+	[[Category: Lin S-X]]
-	~~[[Category: Akr]]~~	+	[[Category: Zhang B]]
-	~~[[Category: Akr1c2]]~~	+
-	~~[[Category: Aldo~~-~~keto reductase~~]]	+
-	[[Category: ~~Alpha~~-~~beta barrel~~]]	+
-	[[Category: ~~Human 3-alpha hds3]]~~	+
-	~~[[Category: Nadph]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 13:02, 16 November 2017

2017-11-16T13:02:19Z

←Older revision		Revision as of 13:02, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='4xo7' size='340' side='right' caption='[[4xo7]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='4xo7' size='340' side='right' caption='[[4xo7]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4xo7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XO7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4xo7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XO7 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l1w\|4l1w]], [[4nnf\|4nnf]], [[4xo6\|4xo6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l1w\|4l1w]], [[4nnf\|4nnf]], [[4xo6\|4xo6]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo7 OCA], [http://pdbe.org/4xo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xo7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xo7 PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AKR1C2, DDH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo7 OCA], [http://pdbe.org/4xo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xo7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xo7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xo7 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Hu, X J]]		[[Category: Hu, X J]]
	[[Category: Lin, S X]]		[[Category: Lin, S X]]

OCA at 17:59, 10 May 2016

2016-05-10T17:59:56Z

←Older revision		Revision as of 17:59, 10 May 2016
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN]] Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.<ref>PMID:8573067</ref>		[[http://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN]] Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.<ref>PMID:8573067</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human 3alpha-HSD3 (3alpha-hydroxysteroid dehydrogenase type 3) plays an essential role in the inactivation of the most potent androgen 5alpha-DHT (5alpha-dihydrotestosterone). The present study attempts to obtain the important structure of 3alpha-HSD3 in complex with 5alpha-DHT and to investigate the role of 3alpha-HSD3 in breast cancer cells. We report the crystal structure of human 3alpha-HSD3.NADP(+).A-dione (5alpha-androstane-3,17-dione)/epi-ADT (epiandrosterone) complex, which was obtained by co-crystallization with 5alpha-DHT in the presence of NADP(+) Although 5alpha-DHT was introduced during the crystallization, oxidoreduction of 5alpha-DHT occurred. The locations of A-dione and epi-ADT were identified in the steroid-binding sites of two 3alpha-HSD3 molecules per crystal asymmetric unit. An overlay showed that A-dione and epi-ADT were oriented upside-down and flipped relative to each other, providing structural clues for 5alpha-DHT reverse binding in the enzyme with the generation of different products. Moreover, we report the crystal structure of the 3alpha-HSD3.NADP(+).4-dione (4-androstene-3,17-dione) complex. When a specific siRNA (100 nM) was used to suppress 3alpha-HSD3 expression without interfering with 3alpha-HSD4, which shares a highly homologous active site, the 5alpha-DHT concentration increased, whereas MCF7 cell growth was suppressed. The present study provides structural clues for 5alpha-DHT reverse binding within 3alpha-HSD3, and demonstrates for the first time that down-regulation of 3alpha-HSD3 decreases MCF7 breast cancer cell growth.
		+
		+	Human 3alpha-hydroxysteroid dehydrogenase type 3: structural clues of 5alpha-DHT reverse binding and enzyme down-regulation decreasing MCF7 cell growth.,Zhang B, Hu XJ, Wang XQ, Theriault JF, Zhu DW, Shang P, Labrie F, Lin SX Biochem J. 2016 Apr 15;473(8):1037-46. doi: 10.1042/BCJ20160083. Epub 2016 Feb, 29. PMID:26929402<ref>PMID:26929402</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4xo7" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:48, 21 February 2016

2016-02-21T02:48:29Z

←Older revision		Revision as of 02:48, 21 February 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 4xo7 is ON HOLD until Paper Publication~~	+	==Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one==
-		+	<StructureSection load='4xo7' size='340' side='right' caption='[[4xo7]], [[Resolution\|resolution]] 1.75Å' scene=''>
-	~~Authors: Zhang, B., Hu, X.-J., Lin, S.-X.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4xo7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XO7 FirstGlance]. <br>
-	~~Description:~~ Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4l1w\|4l1w]], [[4nnf\|4nnf]], [[4xo6\|4xo6]]</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo7 OCA], [http://pdbe.org/4xo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xo7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xo7 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN]] Defects in AKR1C2 are a cause of 46,XY sex reversal type 8 (SRXY8) [MIM:[http://omim.org/entry/614279 614279]]. A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.<ref>PMID:21802064</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AK1C2_HUMAN AK1C2_HUMAN]] Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.<ref>PMID:8573067</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hu, X J]]
		+	[[Category: Lin, S X]]
	[[Category: Zhang, B]]		[[Category: Zhang, B]]
-	[[Category: ~~Lin, S.~~-X]]	+	[[Category: Akr]]
-	[[Category: ~~Hu, X.~~-J]]	+	[[Category: Akr1c2]]
		+	[[Category: Aldo-keto reductase]]
		+	[[Category: Alpha-beta barrel]]
		+	[[Category: Human 3-alpha hds3]]
		+	[[Category: Nadph]]
		+	[[Category: Oxidoreductase]]

OCA at 08:44, 30 April 2015

2015-04-30T08:44:02Z

←Older revision		Revision as of 08:44, 30 April 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4xo7 is ON HOLD	+	The entry 4xo7 is ON HOLD until Paper Publication

	Authors: Zhang, B., Hu, X.-J., Lin, S.-X.		Authors: Zhang, B., Hu, X.-J., Lin, S.-X.

OCA at 11:31, 18 February 2015

2015-02-18T11:31:32Z

←Older revision		Revision as of 11:31, 18 February 2015
Line 3:		Line 3:
	The entry 4xo7 is ON HOLD		The entry 4xo7 is ON HOLD

-	Authors: Zhang, B., Hu, X.-j., Lin, S.-x.	+	Authors: Zhang, B., Hu, X.-J., Lin, S.-X.

-	Description: ~~CRYSTAL STRUCTUER OF HUMAN~~ 3-~~ALPHA HYDROXYSTEROID DEHYDROGENASE TYPE~~ 3 ~~IN COMPLEX WITH~~ NADP+, ~~5ALPHA~~-~~ANDROSTAN~~-3,17-~~DIONE AND~~ (~~3BETA~~, ~~5ALPHA~~)-3-~~HYDROXYANDROSTAN~~-17-~~ONE~~	+	Description: Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Zhang, B]]		[[Category: Zhang, B]]
	[[Category: Lin, S.-X]]		[[Category: Lin, S.-X]]
	[[Category: Hu, X.-J]]		[[Category: Hu, X.-J]]

OCA: Protected "4xo7" [edit=sysop:move=sysop]

2015-01-21T16:05:32Z

Protected "4xo7" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:05, 21 January 2015

OCA: New page: '''Unreleased structure''' The entry 4xo7 is ON HOLD Authors: Zhang, B., Hu, X.-j., Lin, S.-x. Description: CRYSTAL STRUCTUER OF HUMAN 3-ALPHA HYDROXYSTEROID DEHYDROGENASE TYPE 3 IN CO...

2015-01-21T16:05:31Z

New page: '''Unreleased structure''' The entry 4xo7 is ON HOLD Authors: Zhang, B., Hu, X.-j., Lin, S.-x. Description: CRYSTAL STRUCTUER OF HUMAN 3-ALPHA HYDROXYSTEROID DEHYDROGENASE TYPE 3 IN CO...

New page

'''Unreleased structure'''

The entry 4xo7 is ON HOLD

Authors: Zhang, B., Hu, X.-j., Lin, S.-x.

Description: CRYSTAL STRUCTUER OF HUMAN 3-ALPHA HYDROXYSTEROID DEHYDROGENASE TYPE 3 IN COMPLEX WITH NADP+, 5ALPHA-ANDROSTAN-3,17-DIONE AND (3BETA, 5ALPHA)-3-HYDROXYANDROSTAN-17-ONE
[[Category: Unreleased Structures]]
[[Category: Zhang, B]]
[[Category: Lin, S.-X]]
[[Category: Hu, X.-J]]