Structural and functional characterization of Runx1, CBF beta, and CBF beta-SMMHC.
Core binding factors (CBFs) are heterodimeric transcription factors consisting of a DNA-binding CBF alpha subunit and non-DNA-binding CBF beta subunit. DNA binding and heterodimerization is mediated by a single domain in the CBF alpha subunit called the Runt domain, while sequences flanking the Runt domain confer other biochemical activities such as transactivation. On the other hand, the heterodimerization domain in CBF beta is the only functional domain that has been identified in this subunit. The biophysical properties of the Runt domain and the CBF beta heterodimerization domain, and the structures of the isolated domains as well as of the Runt domain-DNA, Runt domain-CBF beta, and ternary Runt domain-CBF beta-DNA complexes, have been characterized over the past several years, and are summarized in this review.
Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Lina
L
Zhang
Stephen M
SM
Lukasik
Nancy A
NA
Speck
John H
JH
Bushweller
D000818:Animals; D001665:Binding Sites; D002151:Calorimetry; D019281:Dimerization; D006801:Humans; D015514:Oncogene Proteins, Fusion / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000235:genetics
C095514:CBFbeta-MYH11 fusion protein; D015514:Oncogene Proteins, Fusion; D011518:Proto-Oncogene Proteins