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1h88
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(New page: 200px<br /> <applet load="1h88" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h88, resolution 2.80Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:07, 12 November 2007
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CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX1
Overview
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.
About this Structure
1H88 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with NH4 as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 17:13:46 2007
