1f93
From Proteopedia
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| - | [[Image:1f93.gif|left|200px]] | + | [[Image:1f93.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH''' | + | {{Structure |
| + | |PDB= 1f93 |SIZE=350|CAPTION= <scene name='initialview01'>1f93</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F93 is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: transcriptional activator/coactivator complex]] | [[Category: transcriptional activator/coactivator complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:06:04 2008'' |
Revision as of 09:06, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH
Overview
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.
About this Structure
1F93 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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