1CMO
IMMUNOGLOBULIN MOTIF DNA-RECOGNITION AND HETERODIMERIZATION FOR THE PEBP2/CBF RUNT-DOMAIN
Summary for 1CMO
Entry DOI | 10.2210/pdb1cmo/pdb |
Descriptor | POLYOMAVIRUS ENHANCER BINDING PROTEIN 2 (1 entity in total) |
Functional Keywords | transcription factor, hematopoiesis, osteogenesis, ig-fold, transcription |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: Q01196 |
Total number of polymer chains | 1 |
Total formula weight | 14008.94 |
Authors | Nagata, T.,Gupta, V.,Sorce, D.,Kim, W.Y.,Sali, A.,Chait, B.T.,Shigesada, K.,Ito, Y.,Werner, M.H. (deposition date: 1999-05-11, release date: 2000-01-05, Last modification date: 2023-12-27) |
Primary citation | Nagata, T.,Gupta, V.,Sorce, D.,Kim, W.Y.,Sali, A.,Chait, B.T.,Shigesada, K.,Ito, Y.,Werner, M.H. Immunoglobulin motif DNA recognition and heterodimerization of the PEBP2/CBF Runt domain. Nat.Struct.Biol., 6:615-618, 1999 Cited by PubMed Abstract: The polyomavirus enhancer binding protein 2 (PEBP2) or core binding factor (CBF) is a heterodimeric enhancer binding protein that is associated with genetic regulation of hematopoiesis and osteogenesis. Aberrant forms of PEBP2/CBF are implicated in the cause of the acute human leukemias and in a disorder of bone development known as cleidocranial dysplasia. The common denominator in the natural and mutant forms of this protein is a highly conserved domain of PEBP2/CBF alpha, termed the Runt domain (RD), which is responsible for both DNA binding and heterodimerization with the beta subunit of PEBP2/CBF. The three-dimensional structure of the RD bound to DNA has been determined to be an S-type immunoglobulin fold, establishing a structural relationship between the RD and the core DNA binding domains of NF-kappaB, NFAT1, p53 and the STAT proteins. NMR spectroscopy of a 43.6 kD RD-beta-DNA ternary complex identified the surface of the RD in contact with the beta subunit, suggesting a mechanism for the enhancement of RD DNA binding by beta. Analysis of leukemogenic mutants within the RD provides molecular insights into the role of this factor in leukemogenesis and cleidocranial dysplasia. PubMed: 10404214DOI: 10.1038/10658 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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