1h89
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1H89 is a | + | 1H89 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: K1 and K2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H89 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription/dna]] | [[Category: transcription/dna]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:56:23 2007'' |
Revision as of 11:51, 5 November 2007
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CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2
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
1H89 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with K as ligand. Structure known Active Sites: K1 and K2. 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 5 13:56:23 2007
