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1gv5
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==CRYSTAL STRUCTURE OF C-MYB R2== |
| + | <StructureSection load='1gv5' size='340' side='right' caption='[[1gv5]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1gv5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GV5 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1guu|1guu]], [[1gv2|1gv2]], [[1h88|1h88]], [[1h89|1h89]], [[1idy|1idy]], [[1idz|1idz]], [[1mbe|1mbe]], [[1mbf|1mbf]], [[1mbg|1mbg]], [[1mbh|1mbh]], [[1mbj|1mbj]], [[1mbk|1mbk]], [[1mse|1mse]], [[1msf|1msf]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gv5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gv5 RCSB], [http://www.ebi.ac.uk/pdbsum/1gv5 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/1gv5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | c-Myb, but not avian myeloblastosis virus (AMV) v-Myb, cooperates with C/EBP beta to regulate transcription of myeloid-specific genes. To assess the structural basis for that difference, we determined the crystal structures of complexes comprised of the c-Myb or AMV v-Myb DNA-binding domain (DBD), the C/EBP beta DBD, and a promoter DNA fragment. Within the c-Myb complex, a DNA-bound C/EBP beta interacts with R2 of c-Myb bound to a different DNA fragment; point mutations in v-Myb R2 eliminate such interaction within the v-Myb complex. GST pull-down assays, luciferase trans-activation assays, and atomic force microscopy confirmed that the interaction of c-Myb and C/EBP beta observed in crystal mimics their long range interaction on the promoter, which is accompanied by intervening DNA looping. | ||
| - | + | Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a promoter.,Tahirov TH, Sato K, Ichikawa-Iwata E, Sasaki M, Inoue-Bungo T, Shiina M, Kimura K, Takata S, Fujikawa A, Morii H, Kumasaka T, Yamamoto M, Ishii S, Ogata K Cell. 2002 Jan 11;108(1):57-70. PMID:11792321<ref>PMID:11792321</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Transcriptional activator|Transcriptional activator]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: Ogata, K.]] | [[Category: Ogata, K.]] | ||
[[Category: Tahirov, T H.]] | [[Category: Tahirov, T H.]] | ||
Revision as of 15:53, 29 September 2014
CRYSTAL STRUCTURE OF C-MYB R2
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