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| | ==AXH domain of the transcription factor HBP1 from M.musculus== | | ==AXH domain of the transcription factor HBP1 from M.musculus== |
| - | <StructureSection load='1v06' size='340' side='right'caption='[[1v06]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1v06' size='340' side='right'caption='[[1v06]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v06]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V06 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v06]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V06 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v06 OCA], [http://pdbe.org/1v06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v06 RCSB], [http://www.ebi.ac.uk/pdbsum/1v06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v06 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v06 OCA], [https://pdbe.org/1v06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v06 RCSB], [https://www.ebi.ac.uk/pdbsum/1v06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v06 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HBP1_MOUSE HBP1_MOUSE] Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the H1F0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4 (By similarity).<ref>PMID:9178770</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chiara, C De]] | + | [[Category: De Chiara C]] |
| - | [[Category: Kelly, G]] | + | [[Category: Kelly G]] |
| - | [[Category: Pastore, A]] | + | [[Category: Pastore A]] |
| - | [[Category: Ataxin-1 homologous]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Nucleic acid binding]]
| + | |
| - | [[Category: Ob-fold]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| - | [[Category: Repressor]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Wnt signaling pathway]]
| + | |
| Structural highlights
Function
HBP1_MOUSE Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the H1F0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4 (By similarity).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
AXH is a protein module identified in two unrelated families that comprise the transcriptional repressor HBP1 and ataxin-1 (ATX1), the protein responsible for spinocerebellar ataxia type-1 (SCA1). SCA1 is a neurodegenerative disorder associated with protein misfolding and formation of toxic intranuclear aggregates. We have solved the structure in solution of monomeric AXH from HBP1. The domain adopts a nonclassical permutation of an OB fold and binds nucleic acids, a function previously unidentified for this region of HBP1. Comparison of HBP1 AXH with the crystal structure of dimeric ATX1 AXH indicates that, despite the significant sequence homology, the two proteins have different topologies, suggesting that AXH has chameleon properties. We further demonstrate that HBP1 AXH remains monomeric, whereas the ATX1 dimer spontaneously aggregates and forms fibers. Our results describe an entirely novel, to our knowledge, example of a chameleon fold and suggest a link between these properties and the SCA1 pathogenesis.
The AXH domain adopts alternative folds the solution structure of HBP1 AXH.,de Chiara C, Menon RP, Adinolfi S, de Boer J, Ktistaki E, Kelly G, Calder L, Kioussis D, Pastore A Structure. 2005 May;13(5):743-53. PMID:15893665[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lavender P, Vandel L, Bannister AJ, Kouzarides T. The HMG-box transcription factor HBP1 is targeted by the pocket proteins and E1A. Oncogene. 1997 Jun 5;14(22):2721-8. PMID:9178770 doi:http://dx.doi.org/10.1038/sj.onc.1201243
- ↑ de Chiara C, Menon RP, Adinolfi S, de Boer J, Ktistaki E, Kelly G, Calder L, Kioussis D, Pastore A. The AXH domain adopts alternative folds the solution structure of HBP1 AXH. Structure. 2005 May;13(5):743-53. PMID:15893665 doi:10.1016/j.str.2005.02.016
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