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Sci. STKE, 1 July 2003
Vol. 2003, Issue 189, p. tw255
[DOI: 10.1126/stke.2003.189.tw255]

EDITORS' CHOICE

PROTEIN DOMAINS Quantitating the Ties That Bind

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]

Citation: Quantitating the Ties That Bind. Sci. STKE 2003, tw255 (2003).

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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)