Summary information and primary citation
- PDB-id
-
1ic8;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (2.6 Å)
- Summary
- Hepatocyte nuclear factor 1a bound to DNA : mody3 gene
product
- Reference
-
Chi Y-I, Frantz JD, Oh B-C, Hansen L, Dhe-Paganon S,
Shoelson SE (2002): "Diabetes
mutations delineate an atypical POU domains in
HNF1-Alpha." Mol.Cell, 10,
1129-1137. doi: 10.1016/S1097-2765(02)00704-9.
- Abstract
- Mutations in Hnf-1alpha are the most common Mendelian
cause of diabetes mellitus. To elucidate the molecular
function of a mutational hotspot, we cocrystallized human
HNF-1alpha 83-279 with a high-affinity promoter and solved
the structure of the complex. Two identical protein
molecules are bound to the promoter. Each contains a
homeodomain and a second domain structurally similar to
POU-specific domains that was not predicted on the basis of
amino acid sequence. Atypical elements in both domains
create a stable interface that further distinguishes
HNF-1alpha from other flexible POU-homeodomain proteins.
The numerous diabetes-causing mutations in HNF-1alpha thus
identified a previously unrecognized POU domain which was
used as a search model to identify additional POU domain
proteins in sequence databases.
