{PDOC51937}
{PS51937; HNF_P1}
{BEGIN}
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* HNF-1 dimerization (HNF-p1) domain profile *
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The homeodomain  proteins hepatocyte nuclear factor (HNF)-1alpha and HNF-1beta
comprise a  functionnally important  family in which dimerization is essential
for DNA  binding.  HNF-1alpha  and HNF-1beta 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-1alpha  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 beta- or
gamma-turn families  (see <PDB:1G39>). The dimer contains a rigid element, the
N-terminal anti-parallel  mini-zipper comprising alpha-helices 1 and 1', and a
plastic element,  the C-terminal coiled-coil comprising alpha-helices 2 and 2'
[2,3,4,5].

The profile we developed covers the entire HNF-p1 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2020 / First entry.

[ 1] Mendel D.B., Crabtree G.R.
     "HNF-1, a member of a novel class of dimerizing homeodomain
     proteins."
     J. Biol. Chem. 266:677-680(1991).
     PubMed=1985954
[ 2] Rose R.B., Bayle J.H., Endrizzi J.A., Cronk J.D., Crabtree G.R.,
     Alber T.
     "Structural basis of dimerization, coactivator recognition and MODY3
     mutations in  HNF-1alpha."
     Nat. Struct. Biol. 7:744-748(2000).
     PubMed=10966642; DOI=10.1038/78966
[ 3] Rose R.B., Endrizzi J.A., Cronk J.D., Holton J., Alber T.
     "High-resolution structure of the HNF-1alpha dimerization domain."
     Biochemistry 39:15062-15070(2000).
     PubMed=11106484; DOI=10.1021/bi001996t
[ 4] Narayana N., Hua Q., Weiss M.A.
     "The dimerization domain of HNF-1alpha: structure and plasticity of an
     intertwined four-helix bundle with application to diabetes mellitus."
     J. Mol. Biol. 310:635-658(2001).
     PubMed=11439029; DOI=10.1006/jmbi.2001.4780
[ 5] Narayana N., Phillips N.B., Hua Q.X., Jia W., Weiss M.A.
     "Diabetes mellitus due to misfolding of a beta-cell transcription
     factor: stereospecific frustration of a Schellman motif in
     HNF-1alpha."
     J. Mol. Biol. 362:414-429(2006).
     PubMed=16930618; DOI=10.1016/j.jmb.2006.06.086

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