1h89
From Proteopedia
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| - | [[Image:1h89.gif|left|200px]] | + | [[Image:1h89.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2''' | + | {{Structure |
| + | |PDB= 1h89 |SIZE=350|CAPTION= <scene name='initialview01'>1h89</scene>, resolution 2.45Å | ||
| + | |SITE= <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> | ||
| + | |LIGAND= <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H89 is a [ | + | 1H89 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H89 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11792321 11792321] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: transcription/dna]] | [[Category: transcription/dna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:33:40 2008'' |
Revision as of 09:33, 20 March 2008
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| , resolution 2.45Å | |||||||
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| Sites: | and | ||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 11:33:40 2008
