1h88: Difference between revisions
New page: left|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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[[Image:1h88.gif|left|200px]]<br /> | [[Image:1h88.gif|left|200px]]<br /><applet load="1h88" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1h88, resolution 2.80Å" /> | caption="1h88, resolution 2.80Å" /> | ||
'''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX1'''<br /> | '''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX1'''<br /> | ||
==Overview== | ==Overview== | ||
c-Myb, but not avian myeloblastosis virus (AMV) v-Myb, cooperates with | 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== | ||
1H88 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 NH4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1H88 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 <scene name='pdbligand=NH4:'>NH4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H88 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ogata, K.]] | [[Category: Ogata, K.]] | ||
[[Category: Tahirov, T | [[Category: Tahirov, T H.]] | ||
[[Category: NH4]] | [[Category: NH4]] | ||
[[Category: bzip]] | [[Category: bzip]] | ||
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[[Category: transcription/dna]] | [[Category: transcription/dna]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:34 2008'' | ||
Revision as of 10:58, 21 February 2008
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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
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