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Sci. Signal., 14 February 2012
Vol. 5, Issue 211, p. ec47
[DOI: 10.1126/scisignal.2002950]

EDITORS' CHOICE

Structural Biology Keeping a Kinase in Check

Valda Vinson

Science, AAAS, Washington, DC 20005, USA

Cyclic adenosine monophosphate (cAMP)–dependent protein kinase (PKA) is involved in the regulation of several key metabolic pathways. It exists in mammalian cells as an inactive tetramer composed of a regulatory (R) subunit dimer and two catalytic (C) subunits. cAMP binding causes activation by releasing the C subunits. Insight into PKA regulation has come from structures of R and C subunit heterodimers; however, further understanding requires knowledge of the holoenzyme structure. P. Zhang et al. report a high-resolution structure of the RIIβ2:C2 tetramer. The structure reveals interactions at an interface between the two RC heterodimers and provides insight into the mechanism of allosteric activation upon cAMP binding.

P. Zhang, E. V. Smith-Nguyen, M. M. Keshwani, M. S. Deal, A. P. Kornev, S. S. Taylor, Structure and allostery of the PKA RIIβ tetrameric holoenzyme. Science 335, 712–716 (2012). [Abstract] [Full Text]

Citation: V. Vinson, Keeping a Kinase in Check. Sci. Signal. 5, ec47 (2012).



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