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1f93

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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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Retrieved from "http://52.214.119.220/wiki/index.php/1f93"

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-[[Image:1f93.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH==
-|PDB= 1f93 |SIZE=350|CAPTION= <scene name='initialview01'>1f93</scene>, resolution 2.60&Aring;
+<StructureSection load='1f93' size='340' side='right'caption='[[1f93]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE=
+<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>
-|DOMAIN=
+<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>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f93 OCA], [http://www.ebi.ac.uk/pdbsum/1f93 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f93 RCSB]</span>
+== Function ==
-}}
+[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>
+== Evolutionary Conservation ==
-'''CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/1f93_consurf.spt"</scriptWhenChecked>
-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.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-F93 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].
+</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].
+<div style="clear:both"></div>
-==Reference==
+== References ==
-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]
+<references/>
-[[Category: Protein complex]]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
 [[Category: Rattus norvegicus]]
-[[Category: Alber, T.]]
+[[Category: Alber T]]
-[[Category: Bayle, J H.]]
+[[Category: Bayle JH]]
-[[Category: Crabtree, G R.]]
+[[Category: Crabtree GR]]
-[[Category: Cronk, J D.]]
+[[Category: Cronk JD]]
-[[Category: Endrizzi, J A.]]
+[[Category: Endrizzi JA]]
-[[Category: Rose, R B.]]
+[[Category: Rose RB]]
-[[Category: dimerization domain]]
-[[Category: four-helix bundle]]
-[[Category: transcriptional activator/coactivator complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:18:14 2008''

1f93

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

Structural highlights

Function

Evolutionary Conservation

References

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