1f17

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{{Seed}}
 
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[[Image:1f17.png|left|200px]]
 
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==L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH==
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The line below this paragraph, containing "STRUCTURE_1f17", creates the "Structure Box" on the page.
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<StructureSection load='1f17' size='340' side='right'caption='[[1f17]], [[Resolution|resolution]] 2.30&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'>[[1f17]] 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=1F17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F17 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]] 2.3&#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=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
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{{STRUCTURE_1f17| PDB=1f17 | 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=1f17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f17 OCA], [https://pdbe.org/1f17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f17 RCSB], [https://www.ebi.ac.uk/pdbsum/1f17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f17 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HCDH_HUMAN HCDH_HUMAN] Defects in HADH are the cause of 3-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH deficiency) [MIM:[https://omim.org/entry/231530 231530]. HADH deficiency is a metabolic disorder with various clinical presentations including hypoglycemia, hepatoencephalopathy, myopathy or cardiomyopathy, and in some cases sudden death. Defects in HADH are the cause of familial hyperinsulinemic hypoglycemia type 4 (HHF4) [MIM:[https://omim.org/entry/609975 609975]; also known as persistent hyperinsulinemic hypoglycemia of infancy (PHHI) or congenital hyperinsulinism. HHF is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. It causes nesidioblastosis, a diffuse abnormality of the pancreas in which there is extensive, often disorganized formation of new islets. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. HHF4 should be easily recognizable by analysis of acylcarnitine species and that this disorder responds well to treatment with diazoxide. It provides the first 'experiment of nature' that links impaired fatty acid oxidation to hyperinsulinism and that provides support for the concept that a lipid signaling pathway is implicated in the control of insulin secretion.<ref>PMID:11489939</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HCDH_HUMAN HCDH_HUMAN] Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.
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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/f1/1f17_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=1f17 ConSurf].
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<div style="clear:both"></div>
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===L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH===
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==See Also==
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 10840044 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_10840044}}
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==About this Structure==
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1F17 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F17 OCA].
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==Reference==
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Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase., Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ, J Biol Chem. 2000 Sep 1;275(35):27186-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10840044 10840044]
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[[Category: 3-hydroxyacyl-CoA dehydrogenase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Banaszak, L J.]]
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[[Category: Banaszak LJ]]
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[[Category: Barycki, J J.]]
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[[Category: Barycki JJ]]
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[[Category: Brien, L K.O.]]
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[[Category: O'Brien LK]]
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[[Category: Strauss, A W.]]
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[[Category: Strauss AW]]
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[[Category: L-3-hydroxyacyl-coa dehydrogenase complexed with nadh]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:19:52 2008''
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Current revision

L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH

PDB ID 1f17

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