1ic8
From Proteopedia
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| - | [[Image:1ic8.gif|left|200px]] | + | [[Image:1ic8.gif|left|200px]] |
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| - | '''HEPATOCYTE NUCLEAR FACTOR 1A BOUND TO DNA : MODY3 GENE PRODUCT''' | + | {{Structure |
| + | |PDB= 1ic8 |SIZE=350|CAPTION= <scene name='initialview01'>1ic8</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HEPATOCYTE NUCLEAR FACTOR 1A BOUND TO DNA : MODY3 GENE PRODUCT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IC8 is a [ | + | 1IC8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IC8 OCA]. |
==Reference== | ==Reference== | ||
| - | Diabetes mutations delineate an atypical POU domain in HNF-1alpha., Chi YI, Frantz JD, Oh BC, Hansen L, Dhe-Paganon S, Shoelson SE, Mol Cell. 2002 Nov;10(5):1129-37. PMID:[http:// | + | Diabetes mutations delineate an atypical POU domain in HNF-1alpha., Chi YI, Frantz JD, Oh BC, Hansen L, Dhe-Paganon S, Shoelson SE, Mol Cell. 2002 Nov;10(5):1129-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12453420 12453420] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation; dna-binding; pou domain; diabetes; disease mutation; mody3]] | [[Category: transcription regulation; dna-binding; pou domain; diabetes; disease mutation; mody3]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:25 2008'' |
Revision as of 09:48, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HEPATOCYTE NUCLEAR FACTOR 1A BOUND TO DNA : MODY3 GENE PRODUCT
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Diabetes mellitus, insulin-dependent OMIM:[142410], Diabetes mellitus, noninsulin-dependent, 2 OMIM:[142410], Hepatic adenoma OMIM:[142410], MODY, type III OMIM:[142410], Renal cell carcinoma OMIM:[142410]
About this Structure
1IC8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Diabetes mutations delineate an atypical POU domain in HNF-1alpha., Chi YI, Frantz JD, Oh BC, Hansen L, Dhe-Paganon S, Shoelson SE, Mol Cell. 2002 Nov;10(5):1129-37. PMID:12453420
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