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1H89

CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2

Summary for 1H89
Entry DOI10.2210/pdb1h89/pdb
Related1H88 1HJB 1IO4
DescriptorCAAT/ENHANCER BINDING PROTEIN BETA, MYB PROTO-ONCOGENE PROTEIN, DNA(5'-(*GP*AP*TP*GP*TP*GP*GP*CP*GP*CP*AP* AP*TP*CP*CP*TP*TP*AP*AP*CP*GP*GP*AP*CP*TP*G)-3'), ... (6 entities in total)
Functional Keywordstranscription/dna, protein-dna complex, transcription regulation, bzip, proto-oncogene, myb, c-myb, c/ebp, transcription-dna complex
Biological sourceHOMO SAPIENS (HUMAN)
More
Total number of polymer chains5
Total formula weight50873.67
Authors
Tahirov, T.H.,Ogata, K. (deposition date: 2001-01-30, release date: 2002-01-28, Last modification date: 2023-12-13)
Primary citationTahirov, T.H.,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.
Mechanism of C-Myb-C/Ebpbeta Cooperation from Separated Sites on a Promoter
Cell(Cambridge,Mass.), 108:57-, 2002
Cited by
PubMed Abstract: 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.
PubMed: 11792321
DOI: 10.1016/S0092-8674(01)00636-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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