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| | ==Crystal Structure Analysis of the UBF HMG box5== | | ==Crystal Structure Analysis of the UBF HMG box5== |
| - | <StructureSection load='2hdz' size='340' side='right' caption='[[2hdz]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2hdz' size='340' side='right'caption='[[2hdz]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hdz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HDZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hdz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HDZ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=2hdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hdz OCA], [http://pdbe.org/2hdz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hdz RCSB], [http://www.ebi.ac.uk/pdbsum/2hdz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hdz ProSAT]</span></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=2hdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hdz OCA], [https://pdbe.org/2hdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hdz RCSB], [https://www.ebi.ac.uk/pdbsum/2hdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hdz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UBF1_HUMAN UBF1_HUMAN]] Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.<ref>PMID:7982918</ref> | + | [https://www.uniprot.org/uniprot/UBF1_HUMAN UBF1_HUMAN] Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.<ref>PMID:7982918</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The fifth HMG-box domain in human upstream binding factor (hUBF) contributes to the synthesis of rRNA by RNA polymerase I (Pol I). The 2.0 A resolution crystal structure of this protein has been solved using the single-wavelength anomalous dispersion method (SAD). The crystal structure and the reported NMR structure have r.m.s. deviations of 2.18-3.03 A for the C(alpha) atoms. However, there are significant differences between the two structures, with displacements of up to 9.0 A. Compared with other HMG-box structures, the r.m.s. deviations for C(alpha) atoms between hUBF HMG box 5 and HMG domains from Drosophila melanogaster protein D and Rattus norvegicus HMG1 are 1.5 and 1.6 A, respectively. This indicates that the differences between the crystal and NMR structures of hUBF HMG box 5 are larger than those with its homologous structures. The differences between the two structures potentially reflect two states with different structures. The specific interactions between the hUBF HMG box 5 and the first bromodomain of TBP-associated factor 1 (TAF1) were studied by ultrasensitive differential scanning calorimetry and chemical shift perturbation. Based on these experimental data, possible sites in hUBF HMG box 5 that may interact with the first bromodomain of TAF1 were proposed.
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| - | Structure of human upstream binding factor HMG box 5 and site for binding of the cell-cycle regulatory factor TAF1.,Rong H, Li Y, Shi X, Zhang X, Gao Y, Dai H, Teng M, Niu L, Liu Q, Hao Q Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):730-7. Epub 2007, May 15. PMID:17505112<ref>PMID:17505112</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 2hdz" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Niu, L W]] | + | [[Category: Large Structures]] |
| - | [[Category: Rong, H]] | + | [[Category: Niu LW]] |
| - | [[Category: Teng, M K]] | + | [[Category: Rong H]] |
| - | [[Category: Hmg domain]] | + | [[Category: Teng MK]] |
| - | [[Category: Protein binding]]
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