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1CMO

IMMUNOGLOBULIN MOTIF DNA-RECOGNITION AND HETERODIMERIZATION FOR THE PEBP2/CBF RUNT-DOMAIN

Summary for 1CMO
Entry DOI10.2210/pdb1cmo/pdb
DescriptorPOLYOMAVIRUS ENHANCER BINDING PROTEIN 2 (1 entity in total)
Functional Keywordstranscription factor, hematopoiesis, osteogenesis, ig-fold, transcription
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q01196
Total number of polymer chains1
Total formula weight14008.94
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 citationNagata, 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: 10404214
DOI: 10.1038/10658
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227561

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