1ic8: Difference between revisions
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|PDB= 1ic8 |SIZE=350|CAPTION= <scene name='initialview01'>1ic8</scene>, resolution 2.6Å | |PDB= 1ic8 |SIZE=350|CAPTION= <scene name='initialview01'>1ic8</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1au7|1AU7]], [[1oct|1OCT]], [[1lfb|1LFB]], [[2lfb|2LFB]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ic8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ic8 OCA], [http://www.ebi.ac.uk/pdbsum/1ic8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ic8 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Oh, B-.C.]] | [[Category: Oh, B-.C.]] | ||
[[Category: Shoelson, S E.]] | [[Category: Shoelson, S E.]] | ||
[[Category: | [[Category: diabetes]] | ||
[[Category: disease mutation]] | |||
[[Category: dna-binding]] | |||
[[Category: mody3]] | |||
[[Category: pou domain]] | |||
[[Category: transcription regulation]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:45 2008'' | ||
