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PROSITE documentation PDOC51937

HNF-1 dimerization (HNF-p1) domain profile





Description

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.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

HNF_P1, PS51937; HNF-1 dimerization (HNF-p1) domain profile  (MATRIX)


References

1AuthorsMendel D.B. Crabtree G.R.
TitleHNF-1, a member of a novel class of dimerizing homeodomain proteins.
SourceJ. Biol. Chem. 266:677-680(1991).
PubMed ID1985954

2AuthorsRose R.B. Bayle J.H. Endrizzi J.A. Cronk J.D. Crabtree G.R. Alber T.
TitleStructural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha.
SourceNat. Struct. Biol. 7:744-748(2000).
PubMed ID10966642
DOI10.1038/78966

3AuthorsRose R.B. Endrizzi J.A. Cronk J.D. Holton J. Alber T.
TitleHigh-resolution structure of the HNF-1alpha dimerization domain.
SourceBiochemistry 39:15062-15070(2000).
PubMed ID11106484
DOI10.1021/bi001996t

4AuthorsNarayana N. Hua Q. Weiss M.A.
TitleThe dimerization domain of HNF-1alpha: structure and plasticity of an intertwined four-helix bundle with application to diabetes mellitus.
SourceJ. Mol. Biol. 310:635-658(2001).
PubMed ID11439029
DOI10.1006/jmbi.2001.4780

5AuthorsNarayana N. Phillips N.B. Hua Q.X. Jia W. Weiss M.A.
TitleDiabetes mellitus due to misfolding of a beta-cell transcription factor: stereospecific frustration of a Schellman motif in HNF-1alpha.
SourceJ. Mol. Biol. 362:414-429(2006).
PubMed ID16930618
DOI10.1016/j.jmb.2006.06.086



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