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1E50

AML1/CBFbeta complex

Summary for 1E50
Entry DOI10.2210/pdb1e50/pdb
DescriptorCORE-BINDING FACTOR ALPHA SUBUNIT, CORE-BINDING FACTOR CBF-BETA (3 entities in total)
Functional Keywordstranscription factor, transcription
Biological sourceHOMO SAPIENS (HUMAN)
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Cellular locationNucleus: Q01196 Q13951
Total number of polymer chains10
Total formula weight152717.52
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 citationWarren, 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: 10856244
DOI: 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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