1h8a
From Proteopedia
(New page: 200px<br /> <applet load="1h8a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h8a, resolution 2.23Å" /> '''CRYSTAL STRUCTURE O...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1h8a.gif|left|200px]]<br /> | + | [[Image:1h8a.gif|left|200px]]<br /><applet load="1h8a" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h8a" size=" | + | |
caption="1h8a, resolution 2.23Å" /> | caption="1h8a, resolution 2.23Å" /> | ||
'''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX3'''<br /> | '''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX3'''<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== | ||
| - | 1H8A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Avian_myeloblastosis_virus Avian myeloblastosis virus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1H8A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Avian_myeloblastosis_virus Avian myeloblastosis virus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8A OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 15: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ogata, K.]] | [[Category: Ogata, K.]] | ||
| - | [[Category: Tahirov, T | + | [[Category: Tahirov, T H.]] |
[[Category: amv]] | [[Category: amv]] | ||
[[Category: avian myeloblastosis virus]] | [[Category: avian myeloblastosis virus]] | ||
| Line 29: | Line 28: | ||
[[Category: v-myb]] | [[Category: v-myb]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:32 2008'' |
Revision as of 10:58, 21 February 2008
|
CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX3
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
1H8A is a Protein complex structure of sequences from Avian myeloblastosis virus and Homo sapiens. 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 Thu Feb 21 12:58:32 2008
