1E50
AML1/CBFbeta complex
Summary for 1E50
Entry DOI | 10.2210/pdb1e50/pdb |
Descriptor | CORE-BINDING FACTOR ALPHA SUBUNIT, CORE-BINDING FACTOR CBF-BETA (3 entities in total) |
Functional Keywords | transcription factor, transcription |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Nucleus: Q01196 Q13951 |
Total number of polymer chains | 10 |
Total formula weight | 152717.52 |
Authors | Warren, A.J.,Bravo, J.,Williams, R.L.,Rabbits, T.H. (deposition date: 2000-07-13, release date: 2001-07-12, Last modification date: 2024-05-08) |
Primary citation | Warren, A.J.,Bravo, J.,Williams, R.L.,Rabbits, T.H. Structural Basis for the Heterodimeric Interaction between the Acute Leukaemia-Associated Transcription Factors Aml1 and Cbfbeta Embo J., 19:3004-, 2000 Cited by PubMed Abstract: Mutations in the genes encoding the interacting proteins AML1 and CBFbeta are the most common genetic abnormalities in acute leukaemia, and congenital mutations in the related AML3 gene are associated with disorders of osteogenesis. Furthermore, the interaction of AML1 with CBFbeta is essential for haematopoiesis. We report the 2.6 A resolution crystal structure of the complex between the AML1 Runt domain and CBFbeta, which represents a paradigm for the mode of interaction of this highly conserved family of transcription factors. The structure demonstrates that point mutations associated with cleidocranial dysplasia map to the conserved heterodimer interface, suggesting a role for CBFbeta in osteogenesis, and reveals a potential protein interaction platform composed of conserved negatively charged residues on the surface of CBFbeta. PubMed: 10856244DOI: 10.1093/EMBOJ/19.12.3004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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