1h89
From Proteopedia
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| - | [[Image:1h89.gif|left|200px]]<br /><applet load="1h89" size=" | + | [[Image:1h89.gif|left|200px]]<br /><applet load="1h89" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h89, resolution 2.45Å" /> | caption="1h89, resolution 2.45Å" /> | ||
'''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2'''<br /> | '''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. Known structural/functional Sites: <scene name='pdbsite=K1:K Binding Site For Residue C1192 Bound To Main-Chain Oxy ...'>K1</scene> and <scene name='pdbsite=K2:K Binding Site For Residue C1193 Bound To Main-Chain Oxy ...'>K2</scene>. Full crystallographic information is available from [http:// | + | 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 <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=K1:K+Binding+Site+For+Residue+C1192+Bound+To+Main-Chain+Oxy+...'>K1</scene> and <scene name='pdbsite=K2:K+Binding+Site+For+Residue+C1193+Bound+To+Main-Chain+Oxy+...'>K2</scene>. Full crystallographic information is available from [http://oca.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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:38 2008'' |
Revision as of 07:47, 3 February 2008
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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 as ligand. Known structural/functional Sites: and . 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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