1h88
From Proteopedia
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|PDB= 1h88 |SIZE=350|CAPTION= <scene name='initialview01'>1h88</scene>, resolution 2.80Å | |PDB= 1h88 |SIZE=350|CAPTION= <scene name='initialview01'>1h88</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH4:AMMONIUM ION'>NH4</scene> | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hjb|1HJB]], [[1h89|1H89]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h88 OCA], [http://www.ebi.ac.uk/pdbsum/1h88 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h88 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ogata, K.]] | [[Category: Ogata, K.]] | ||
[[Category: Tahirov, T H.]] | [[Category: Tahirov, T H.]] | ||
| - | [[Category: NH4]] | ||
[[Category: bzip]] | [[Category: bzip]] | ||
[[Category: c-myb]] | [[Category: c-myb]] | ||
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[[Category: transcription/dna]] | [[Category: transcription/dna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:50 2008'' |
Revision as of 17:59, 30 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Related: | 1HJB, 1H89
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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