1H9D

Aml1/cbf-beta/dna complex

Summary for 1H9D

• Entry DOI: 10.2210/pdb1h9d/pdb
• Related: 1CL3 1CMO 1CO1 1E50
• Descriptor: CORE-BINDING FACTOR ALPHA SUBUNIT1, CORE-BINDING FACTOR CBF-BETA, DNA (5'-(*GP*TP*TP*GP*CP*GP*GP*TP*TP*G)-3'), ... (5 entities in total)
• Functional Keywords: transcription factor
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: Q01196 Q13951
• Total number of polymer chains: 8
• Total formula weight: 73629.69

Authors

Bravo, J.,Warren, A.J. (deposition date: 2001-03-07, release date: 2001-03-31, Last modification date: 2023-12-13)

Primary citation

Bravo, J.,Li, Z.,Speck, N.A.,Warren, A.J.
The Leukemia-Associated Aml1 (Runx1)-Cbfbeta Complex Functions as a DNA-Induced Molecular Clamp
Nat.Struct.Biol., 8:371-, 2001

PubMed Abstract: 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.

PubMed: 11276260
DOI: 10.1038/86264

Experimental method

X-RAY DIFFRACTION (2.6 Å)