Crystal Structure of Dimerization Domain (1-33) of HNF-1alpha
The dimerization domain of HNF-1alpha: structure and plasticity of an intertwined four-helix bundle with application to diabetes mellitus.
Diabetes-Associated Mutations in a beta-Cell Transcription factor Destabilize an Antiparallel "Mini-Zipper" in a Dimerization Interface
Structural Basis of Dimerization, Coactivator Recognition and MODY3 Mutations in HNF-1alpha
High-Resolution Structure of the HNF-1alpha Dimerization Domain
HNF1, A Homeoprotein Member of the Hepatic Transcription Regulatory Network
Maturity-onset Diabetes of the Young (MODY), MODY Genes and Non-Insulin-Dependent Diabetes mellitus
MPD, Tris-HCl, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
1g39 is the structure of the wild-type dimerization domain
1g2y is the structure of the variant peptide with L12 replaced by seleno-methionine
1g2z is the structure of the same peptide with L13 replaced by seleno-methionine.
1f93 is the structure of the wild-type dimerization domain complexed with DCoH
This peptide was chemically synthesized. The sequence of this peptide occurs naturally in Mus musculus (mouse) as well as in Homo sapiens (humans).
There are two independent molecules in the asymmetric unit. For each molecule, a crystallographic 2-fold axis generates the biological dimer.
Four-helix bundle, non-canonical turn, TRANSCRIPTION