|PROSITE documentation PDOC51937|
The homeodomain proteins hepatocyte nuclear factor (HNF)-1α and HNF-1β comprise a functionnally important family in which dimerization is essential for DNA binding. HNF-1α and HNF-1β regulate tissue-specific genes in liver, kidney, intestine, and pancreas. These proteins form homo- and heterodimers through an autonomously folded domain encompassing the 32 N-terminal amino acids (HNF-p1). The dimerization domain also binds the transcriptional coactivator DCoH, which stimulates HNF-1α activity [1,2,3,4,5].
The HNF-p1 dimer folds into an X-type, antiparallel, four-helix bundle (4HB). Each monomer consists of two helices: a longer N-terminal helix and a shorter C-terminal helix, connected by a tight turn unrelated to classical β- or γ-turn families (see <PDB:1G39>). The dimer contains a rigid element, the N-terminal anti-parallel mini-zipper comprising α-helices 1 and 1', and a plastic element, the C-terminal coiled-coil comprising α-helices 2 and 2' [2,3,4,5].
The profile we developed covers the entire HNF-p1 domain.Last update:
August 2020 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Mendel D.B. Crabtree G.R.|
|Title||HNF-1, a member of a novel class of dimerizing homeodomain proteins.|
|Source||J. Biol. Chem. 266:677-680(1991).|
|2||Authors||Rose R.B. Bayle J.H. Endrizzi J.A. Cronk J.D. Crabtree G.R. Alber T.|
|Title||Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha.|
|Source||Nat. Struct. Biol. 7:744-748(2000).|
|3||Authors||Rose R.B. Endrizzi J.A. Cronk J.D. Holton J. Alber T.|
|Title||High-resolution structure of the HNF-1alpha dimerization domain.|
|4||Authors||Narayana N. Hua Q. Weiss M.A.|
|Title||The dimerization domain of HNF-1alpha: structure and plasticity of an intertwined four-helix bundle with application to diabetes mellitus.|
|Source||J. Mol. Biol. 310:635-658(2001).|
|5||Authors||Narayana N. Phillips N.B. Hua Q.X. Jia W. Weiss M.A.|
|Title||Diabetes mellitus due to misfolding of a beta-cell transcription factor: stereospecific frustration of a Schellman motif in HNF-1alpha.|
|Source||J. Mol. Biol. 362:414-429(2006).|