1HJC

CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER

Summary for 1HJC

• Entry DOI: 10.2210/pdb1hjc/pdb
• Related: 1CMO 1CO1 1E50 1HJB 1IO4
• Descriptor: RUNT-RELATED TRANSCRIPTION FACTOR 1, DNA (5'-(*GP*AP*AP*CP*TP*CP*TP*GP*TP*GP*GP* TP*TP*GP*CP*G)-3'), DNA (5'-(CP*CP*GP*CP*AP*AP*CP*CP*AP*CP*AP* GP*AP*GP*TP*T)-3'), ... (4 entities in total)
• Functional Keywords: transcription/dna, protein-dna complex, transcription factor, bzip, runx, runt, c/ebp, cbf, core binding factor, aml1, aml, oncoprotein, transcription-dna complex
• Biological source: MUS MUSCULUS (MOUSE); More
• Total number of polymer chains: 6
• Total formula weight: 47026.13

Authors

Tahirov, T.H.,Ogata, K. (deposition date: 2001-01-11, release date: 2001-03-09, Last modification date: 2023-12-13)

Primary citation

Tahirov, T.H.,Inoue-Bungo, T.,Morii, H.,Fujikawa, A.,Sasaki, M.,Kimura, K.,Shiina, M.,Sato, K.,Kumasaka, T.,Yamamoto, M.,Ishii, S.,Ogata, K.
Structural Analyses of DNA Recognition by the Aml1/Runx-1 Runt Domain and its Allosteric Control by Cbfbeta
Cell(Cambridge,Mass.), 104:755-, 2001

PubMed Abstract: The core binding factor (CBF) heterodimeric transcription factors comprised of AML/CBFA/PEBP2alpha/Runx and CBFbeta/PEBP2beta subunits are essential for differentiation of hematopoietic and bone cells, and their mutation is intimately related to the development of acute leukemias and cleidocranial dysplasia. Here, we present the crystal structures of the AML1/Runx-1/CBFalpha(Runt domain)-CBFbeta(core domain)-C/EBPbeta(bZip)-DNA, AML1/Runx-1/CBFalpha(Runt domain)-C/EBPbeta(bZip)-DNA, and AML1/Runx-1/CBFalpha(Runt domain)-DNA complexes. The hydrogen bonding network formed among CBFalpha(Runt domain) and CBFbeta, and CBFalpha(Runt domain) and DNA revealed the allosteric regulation mechanism of CBFalpha(Runt domain)-DNA binding by CBFbeta. The point mutations of CBFalpha related to the aforementioned diseases were also mapped and their effect on DNA binding is discussed.

PubMed: 11257229
DOI: 10.1016/S0092-8674(01)00271-9

Experimental method

X-RAY DIFFRACTION (2.65 Å)