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1q5m

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[[Image:1q5m.gif|left|200px]]
 
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==Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH==
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The line below this paragraph, containing "STRUCTURE_1q5m", creates the "Structure Box" on the page.
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<StructureSection load='1q5m' size='340' side='right'caption='[[1q5m]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1q5m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q5M FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.32&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1q5m| PDB=1q5m | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5m OCA], [https://pdbe.org/1q5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q5m RCSB], [https://www.ebi.ac.uk/pdbsum/1q5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q5m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PE2R_RABIT PE2R_RABIT] Can convert prostaglandin E2 to prostaglandin F2-alpha.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q5/1q5m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q5m ConSurf].
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<div style="clear:both"></div>
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'''Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH'''
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==See Also==
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*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The aldo-keto reductase rabbit 20alpha-hydroxysteroid dehydrogenase (rb20alpha-HSD; AKR1C5) is less selective than other HSDs, since it exerts its activity both on androgens (C19 steroids) and progestins (C21 steroids). In order to identify the molecular determinants responsible for this reduced selectivity, binary (NADPH) and ternary (NADP(+)/testosterone) complex structures were solved to 1.32A and 2.08A resolution, respectively. Inspection of the cofactor-binding cavity led to the identification of a new interaction between side-chains of residues His222 and Lys270, which cover the central phosphate chain of the cofactor, reminiscent of the "safety-belt" found in other aldo-keto reductases. Testosterone is stabilized by a phenol/benzene tunnel composed of side-chains of numerous residues, among which Phe54, which forces the steroid to take up an orientation markedly contrasting with that found in HSD ternary complexes reported. Combining structural, site-directed mutagenesis, kinetic and fluorescence titration studies, we found that the selectivity of rb20alpha-HSD is mediated by (i) the relaxation of loop B (residues 223-230), partly controlled by the nature of residue 230, (ii) the nature of the residue found at position 54, and (iii) the residues found in the C-terminal tail of the protein especially the side-chain of the amino acid 306.
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[[Category: Large Structures]]
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==About this Structure==
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1Q5M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5M OCA].
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==Reference==
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Loop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamily., Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton R, J Mol Biol. 2004 May 21;339(1):89-102. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15123423 15123423]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Breton R]]
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[[Category: Breton, R.]]
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[[Category: Cantin L]]
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[[Category: Cantin, L.]]
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[[Category: Couture JF]]
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[[Category: Couture, J F.]]
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[[Category: Labrie F]]
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[[Category: Labrie, F.]]
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[[Category: Legrand P]]
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[[Category: Legrand, P.]]
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[[Category: Luu-The V]]
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[[Category: Luu-The, V.]]
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[[Category: Aldo-keto reductase]]
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[[Category: Hsd]]
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[[Category: Hydroxysteroid dehydrogenase]]
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[[Category: Nadph]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:53:30 2008''
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Current revision

Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH

PDB ID 1q5m

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