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1e50

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{{STRUCTURE_1e50| PDB=1e50 | SCENE= }}
{{STRUCTURE_1e50| PDB=1e50 | SCENE= }}
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'''AML1/CBF COMPLEX'''
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===AML1/CBF COMPLEX===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10856244}}
==Disease==
==Disease==
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[[Category: Williams, R L.]]
[[Category: Williams, R L.]]
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Revision as of 21:09, 30 June 2008

Image:1e50.png

Template:STRUCTURE 1e50

Contents

AML1/CBF COMPLEX

Template:ABSTRACT PUBMED 10856244

Disease

Known disease associated with this structure: Leukemia, acute myeloid OMIM:[151385], Platelet disorder, familial, with associated myeloid malignancy OMIM:[151385], Rheumatoid arthritis, susceptibility to OMIM:[151385]

About this Structure

1E50 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the heterodimeric interaction between the acute leukaemia-associated transcription factors AML1 and CBFbeta., Warren AJ, Bravo J, Williams RL, Rabbitts TH, EMBO J. 2000 Jun 15;19(12):3004-15. PMID:10856244

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