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| - | [[Image:1ru0.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ru0| PDB=1ru0 | SCENE= }} | | {{STRUCTURE_1ru0| PDB=1ru0 | SCENE= }} |
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| - | '''Crystal structure of DCoH2, a paralog of DCoH, the Dimerization Cofactor of HNF-1'''
| + | ===Crystal structure of DCoH2, a paralog of DCoH, the Dimerization Cofactor of HNF-1=== |
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| - | ==Overview==
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| - | An inherited form of diabetes, maturity-onset diabetes of the young type 3 (MODY3), results from mutations in the transcriptional activator, hepatocyte nuclear factor-1alpha (HNF1alpha). Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1). Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion. It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion. To test this idea, we determined the biochemical properties and the 1.6-A-resolution crystal structure of DCoH2. Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro. DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface. In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro. Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans. These results suggest distinct roles for DCoH and DCoH2. Differences in conserved surface residues could mediate binding to different effectors. We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15182178}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15182178 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15182178}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rose, R B.]] | | [[Category: Rose, R B.]] |
| | [[Category: Alpha and beta structure]] | | [[Category: Alpha and beta structure]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:54:22 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:49:11 2008'' |
Revision as of 17:49, 28 July 2008
Template:STRUCTURE 1ru0
Crystal structure of DCoH2, a paralog of DCoH, the Dimerization Cofactor of HNF-1
Template:ABSTRACT PUBMED 15182178
About this Structure
1RU0 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2., Rose RB, Pullen KE, Bayle JH, Crabtree GR, Alber T, Biochemistry. 2004 Jun 15;43(23):7345-55. PMID:15182178
Page seeded by OCA on Mon Jul 28 20:49:11 2008
