1dcp: Difference between revisions

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


{{Structure
<!--
|PDB= 1dcp |SIZE=350|CAPTION= <scene name='initialview01'>1dcp</scene>, resolution 2.30&Aring;
The line below this paragraph, containing "STRUCTURE_1dcp", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
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|DOMAIN=
{{STRUCTURE_1dcp| PDB=1dcp  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://www.ebi.ac.uk/pdbsum/1dcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB]</span>
}}


'''DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN'''
'''DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN'''
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[[Category: Endrizzi, J A.]]
[[Category: Endrizzi, J A.]]
[[Category: 4a-carbinolamine dehydratase]]
[[Category: 4a-carbinolamine dehydratase]]
[[Category: dehydratase]]
[[Category: Dehydratase]]
[[Category: dimerization cofactor]]
[[Category: Dimerization cofactor]]
[[Category: transcriptional stimulator]]
[[Category: Transcriptional stimulator]]
[[Category: transregulator of homeodomain protein]]
[[Category: Transregulator of homeodomain protein]]
 
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Revision as of 13:42, 2 May 2008

File:1dcp.jpg

Template:STRUCTURE 1dcp

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


OverviewOverview

DCoH, the dimerization cofactor of hepatocyte nuclear factor 1 (HNF-1), functions as both a transcriptional coactivator and a pterin dehydratase. To probe the relationship between these two functions, the X-ray crystal structures of the free enzyme and its complex with the product analogue 7,8-dihydrobiopterin were refined at 2.3 A resolution. The ligand binds at four sites per tetrameric enzyme, with little apparent conformational change in the protein. Each active-site cleft is located in a subunit interface, adjacent to a prominent saddle motif that has structural similarities to the TATA binding protein. The pterin binds within an arch of aromatic residues that extends across one dimer interface. The bound ligand makes contacts to three conserved histidines, and this arrangement restricts proposals for the enzymatic mechanism of dehydration. The dihedral symmetry of DCoH suggests that binding to the dimerization domain of HNF-1 likely involves the superposition of two-fold rotation axes of the two proteins.

About this StructureAbout this Structure

1DCP is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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:8897596 Page seeded by OCA on Fri May 2 13:41:59 2008

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