Protein Domains

Quantitating the Ties That Bind

Science's STKE  01 Jul 2003:
Vol. 2003, Issue 189, pp. tw255-TW255
DOI: 10.1126/stke.2003.189.tw255

The ability of leucine zipper-containing proteins (bZIP proteins) to form homo- and heterodimers increases their selectivity and diversity. To help determine the basis for their interactions, Newman and Keating used protein arrays to analyze the ability of 49 of 51 human bZIP proteins to dimerize in all possible pairwise combinations. Reciprocal binding analyses and biophysical studies in solution were used to confirm the validity of the interactions. New associations were observed that could be related to the functioning of the circadian clock and an intracellular signaling pathway that responds to unfolded proteins.

J. R. S. Newman, A. E. Keating, Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science 300, 2097-2101 (2003). [Abstract] [Full Text]