Diabetes mutations delineate an atypical POU domain in HNF-1alpha.

@article{Chi2002DiabetesMD,
  title={Diabetes mutations delineate an atypical POU domain in HNF-1alpha.},
  author={Young-In Chi and James Daniel Frantz and Byung-Chul Oh and Lone Hansen and Sirano dhe-Paganon and Steven E. Shoelson},
  journal={Molecular cell},
  year={2002},
  volume={10 5},
  pages={
          1129-37
        }
}
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… CONTINUE READING

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