This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ic8
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Diabetes mellitus, insulin-dependent OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142410 142410]], Diabetes mellitus, noninsulin-dependent, 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142410 142410]], Hepatic adenoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142410 142410]], MODY, type III OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142410 142410]], Renal cell carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142410 142410]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 31: | Line 31: | ||
[[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'' |
Revision as of 18:17, 30 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1AU7, 1OCT, 1LFB, 2LFB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HEPATOCYTE NUCLEAR FACTOR 1A BOUND TO DNA : MODY3 GENE PRODUCT
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.
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
Page seeded by OCA on Sun Mar 30 21:17:45 2008
