1f93

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{{Seed}}
 
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[[Image:1f93.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH==
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The line below this paragraph, containing "STRUCTURE_1f93", creates the "Structure Box" on the page.
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<StructureSection load='1f93' size='340' side='right'caption='[[1f93]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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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'>[[1f93]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F93 FirstGlance]. <br>
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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]] 2.6&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1f93| PDB=1f93 | 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=1f93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f93 OCA], [https://pdbe.org/1f93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f93 RCSB], [https://www.ebi.ac.uk/pdbsum/1f93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f93 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHS_RAT PHS_RAT] Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.<ref>PMID:1763325</ref> <ref>PMID:8444860</ref>
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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/f9/1f93_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1f93 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Maturity-onset diabetes of the young type 3 (MODY3) results from mutations in the transcriptional activator hepatocyte nuclear factor-1alpha (HNF-1alpha). Several MODY3 mutations target the HNF-1alpha dimerization domain (HNF-p1), which binds the coactivator, dimerization cofactor of HNF-1 (DCoH). To define the mechanism of coactivator recognition and the basis for the MODY3 phenotype, we determined the cocrystal structure of the DCoH-HNF-p1 complex and characterized biochemically the effects of MODY3 mutations in HNF-p1. The DCoH-HNF-p1 complex comprises a dimer of dimers in which HNF-p1 forms a unique four-helix bundle. Through rearrangements of interfacial side chains, a single, bifunctional interface in the DCoH dimer mediates both HNF-1alpha binding and formation of a competing, transcriptionally inactive DCoH homotetramer. Consistent with the structure, MODY3 mutations in HNF-p1 reduce activator function by two distinct mechanisms.
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===CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH===
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Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha.,Rose RB, Bayle JH, Endrizzi JA, Cronk JD, Crabtree GR, Alber T Nat Struct Biol. 2000 Sep;7(9):744-8. PMID:10966642<ref>PMID:10966642</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_10966642}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1f93" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10966642 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10966642}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1F93 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F93 OCA].
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[[Category: Mus musculus]]
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==Reference==
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Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha., Rose RB, Bayle JH, Endrizzi JA, Cronk JD, Crabtree GR, Alber T, Nat Struct Biol. 2000 Sep;7(9):744-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10966642 10966642]
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[[Category: Protein complex]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Alber, T.]]
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[[Category: Alber T]]
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[[Category: Bayle, J H.]]
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[[Category: Bayle JH]]
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[[Category: Crabtree, G R.]]
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[[Category: Crabtree GR]]
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[[Category: Cronk, J D.]]
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[[Category: Cronk JD]]
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[[Category: Endrizzi, J A.]]
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[[Category: Endrizzi JA]]
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[[Category: Rose, R B.]]
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[[Category: Rose RB]]
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[[Category: Dimerization domain]]
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[[Category: Four-helix bundle]]
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[[Category: Transcriptional activator/coactivator complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:53:39 2008''
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Current revision

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH

PDB ID 1f93

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