The Zinc Finger-Associated SCAN Box Is a Conserved Oligomerization Domain

Abstract

A number of Cys₂His₂ zinc finger proteins contain a highly conserved amino-terminal motif termed the SCAN domain. This element is an 80-residue, leucine-rich region that contains three segments strongly predicted to be α-helices. In this report, we show that the SCAN motif functions as an oligomerization domain mediating self-association or association with other proteins bearing SCAN domains. These findings suggest that the SCAN domain plays an important role in the assembly and function of this newly defined subclass of transcriptional regulators.

ACKNOWLEDGMENTS

We thank Michelle Spotnitz for assistance with the calculation of the phylogenetic tree.

These studies were supported by NIH grants R37 HL35716 and HL61001. S.C.B. is a Pew Scholar in the Biomedical Sciences.