1gv5: Difference between revisions
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<StructureSection load='1gv5' size='340' side='right'caption='[[1gv5]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='1gv5' size='340' side='right'caption='[[1gv5]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == 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 [ | <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 [https://proteopedia.org/fgij/fg.htm?mol=1GV5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='related'><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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gv5 OCA], [https://pdbe.org/1gv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gv5 RCSB], [https://www.ebi.ac.uk/pdbsum/1gv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gv5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/MYB_MOUSE MYB_MOUSE]] Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Transcriptional activator|Transcriptional activator]] | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:24, 17 February 2021
CRYSTAL STRUCTURE OF C-MYB R2CRYSTAL STRUCTURE OF C-MYB R2
Structural highlights
Function[MYB_MOUSE] Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. 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 PubMedc-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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