1gu5: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 <StructureSection load='1gu5' size='340' side='right' caption='[[1gu5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gu5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GU5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gu5]] is a 4 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=1GU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GU5 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gtw|1gtw]], [[1gu4|1gu4]], [[1h88|1h88]], [[1h89|1h89]], [[1h8a|1h8a]], [[1hjb|1hjb]], [[1io4|1io4]]</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=1gu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu5 OCA], [http://pdbe.org/1gu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gu5 RCSB], [http://www.ebi.ac.uk/pdbsum/1gu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu5 ProSAT]</span></td></tr>
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 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/1gu5_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/1gu5_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
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 <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.
+Three types of protein-DNA complexes, AML1/Runx-1/CBFalpha(Runt)-CBFbeta-C/EBPbeta(bZip)-DNA (CBFalpha-beta-C/EBPbeta-DNA), AML1/Runx-1/CBFalpha(Runt)-C/EBPbeta(bZip)-DNA (CBFalpha-C/EBPbeta-DNA) and AML1/Runx-1/CBFalpha(Runt)-DNA (CBFalpha-DNA), were crystallized. The crystals were all orthorhombic and belonged to space groups C222(1), P2(1)2(1)2 and P2(1)2(1)2(1), respectively. The resolutions of CBFalpha-beta-C/EBPbeta-DNA and CBFalpha-C/EBPbeta-DNA crystals were both 3 A, while that of the CBFalpha-DNA crystal was 2.65 A. Complete data sets were collected for all of the native crystals, along with MAD and MIR data sets for CBFalpha-beta-C/EBPbeta-DNA. The heavy-atom site was determined using MAD data for a gold derivative of CBFalpha-beta-C/EBPbeta-DNA.
-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>
+Crystallization and preliminary X-ray analyses of quaternary, ternary and binary protein-DNA complexes with involvement of AML1/Runx-1/CBFalpha Runt domain, CBFbeta and the C/EBPbeta bZip region.,Tahirov TH, Inoue-Bungo T, Sasaki M, Shiina M, Kimura K, Sato K, Kumasaka T, Yamamoto M, Kamiya N, Ogata K Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):850-3. Epub 2001, May 25. PMID:11375505<ref>PMID:11375505</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Ogata, K]]
 [[Category: Tahirov, T H]]