1h9d
From Proteopedia
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AML1/CBF-BETA/DNA COMPLEX
Contents |
Overview
We have determined the structure, at 2.6 A resolution, of the AML1 (Runx1), Runt domain--CBF beta--DNA ternary complex, the most common target for, mutations in human leukemia. The structure reveals that the Runt domain, DNA binding mechanism is unique within the p53 family of transcription, factors. The extended C-terminal 'tail' and 'wing' elements adopt a, specific DNA-bound conformation that clamps the phosphate backbone between, the major and minor grooves of the distorted B-form DNA recognition site., Furthermore, the extended 'tail' mediates most of the NF-kappa B/Rel-like, base-specific contacts in the major groove. The structure clearly explains, the molecular basis for the loss of DNA binding function of the Runt, domain--CBF beta complex as a consequence of the human disease-associated, mutations in leukemogenesis and cleidocranial dysplasia.
Disease
Known diseases associated with this structure: Leukemia, acute myeloid OMIM:[151385], Myeloid leukemia, acute, M4Eo subtype OMIM:[121360], Platelet disorder, familial, with associated myeloid malignancy OMIM:[151385], Rheumatoid arthritis, susceptibility to OMIM:[151385]
About this Structure
1H9D is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The leukemia-associated AML1 (Runx1)--CBF beta complex functions as a DNA-induced molecular clamp., Bravo J, Li Z, Speck NA, Warren AJ, Nat Struct Biol. 2001 Apr;8(4):371-8. PMID:11276260
Page seeded by OCA on Mon Nov 12 17:14:16 2007
