1dcp: Difference between revisions

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[[Image:1dcp.png|left|200px]]


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==DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN==
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<StructureSection load='1dcp' size='340' side='right'caption='[[1dcp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. The August 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCP 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]] 2.3&#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=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>
{{STRUCTURE_1dcp|  PDB=1dcp  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [https://pdbe.org/1dcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [https://www.ebi.ac.uk/pdbsum/1dcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcp ProSAT]</span></td></tr>
 
</table>
===DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN===
== 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 ==
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==About this Structure==
  </jmolCheckbox>
1DCP is a [[Single protein]] structure of sequence 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=1DCP 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=1dcp ConSurf].
 
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==Reference==
== References ==
High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue., Cronk JD, Endrizzi JA, Alber T, Protein Sci. 1996 Oct;5(10):1963-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8897596 8897596]
<references/>
[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Tetrahydrobiopterin Biosynthesis]]
[[Category: Alber, T.]]
[[Category: Alber T]]
[[Category: Cronk, J D.]]
[[Category: Cronk JD]]
[[Category: Endrizzi, J A.]]
[[Category: Endrizzi JA]]
[[Category: 4a-carbinolamine dehydratase]]
[[Category: Dehydratase]]
[[Category: Dimerization cofactor]]
[[Category: Transcriptional stimulator]]
[[Category: Transregulator of homeodomain protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:49:51 2008''

Latest revision as of 06:52, 7 February 2024

DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN

1dcp, resolution 2.30Å

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