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1f93
From Proteopedia
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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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