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Letter
Nature Structural Biology  6, 615 - 619 (1999)
doi:10.1038/10658

Immunoglobulin motif DNA recognition and heterodimerization of the PEBP2/CBF Runt domain

Takashi Nagata1, 2, Vineet Gupta1, 2, Damian Sorce2, Woo-Young Kim3, Andrej Sali2, Brian T. Chait4, Katsuya Shigesada3, Yoshiaki Ito3 & Milton H. Werner2

1  These authors contributed equally to this work.

2  Laboratories of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, Box 42, New York, NY 10021, USA.

3  Institute for Virus Research, Kyoto University, Japan.

4  Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, 1230 York Avenue, Box 42, New York, NY 10021, USA.

Correspondence should be addressed to Milton H. Werner mwerner@portugal.rockefeller.edu
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/CBFalpha, 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.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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