Structure and Allostery of the PKA Rllβ Tetrameric Holoenzyme
Structure and Allostery of the PKA Rllβ Tetrameric Holoenzyme
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Publisher
American Association for the Advancement of Science
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Language
English
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Publisher
American Association for the Advancement of Science
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Contents
In its physiological state, cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) is a tetramer that contains a regulatory (R) subunit dimer and two catalytic (C) subunits.We describe here the 2.3 angstrom structure of full-length tetrameric Rllß₂: C₂ holoenzyme. This structure showing a dimer of dimers provides a mechanistic underst...
Alternative Titles
Full title
Structure and Allostery of the PKA Rllβ Tetrameric Holoenzyme
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TN_cdi_jstor_primary_41487322
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_41487322
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ISSN
0036-8075
E-ISSN
1095-9203
