1IC8

HEPATOCYTE NUCLEAR FACTOR 1A BOUND TO DNA : MODY3 GENE PRODUCT

Summary for 1IC8

• Entry DOI: 10.2210/pdb1ic8/pdb
• Related: 1AU7 1LFB 1OCT 2LFB
• Descriptor: 5'-D(*CP*TP*TP*GP*GP*TP*TP*AP*AP*TP*AP*AP*TP*TP*CP*AP*CP*CP*AP*GP*A)-3', 5'-D(*TP*CP*TP*GP*GP*TP*GP*AP*AP*TP*TP*AP*TP*TP*AP*AP*CP*CP*AP*AP*G)-3', HEPATOCYTE NUCLEAR FACTOR 1-ALPHA, ... (4 entities in total)
• Functional Keywords: transcription regulation; dna-binding; pou domain; diabetes; disease mutation; mody3, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : P20823
• Total number of polymer chains: 4
• Total formula weight: 57857.03

Authors

Chi, Y.-I.,Frantz, J.D.,Oh, B.-C.,Hansen, L.,Dhe-Paganon, S.,Shoelson, S.E. (deposition date: 2001-03-30, release date: 2002-11-27, Last modification date: 2024-02-07)

Primary citation

Chi, Y.-I.,Frantz, J.D.,Oh, B.-C.,Hansen, L.,Dhe-Paganon, S.,Shoelson, S.E.
Diabetes mutations delineate an atypical POU domains in HNF1-Alpha
Mol.Cell, 10:1129-1137, 2002

PubMed 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.

PubMed: 12453420
DOI: 10.1016/S1097-2765(02)00704-9

Experimental method

X-RAY DIFFRACTION (2.6 Å)