Protein Kinase A: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Hakyong Kwak, Michal Harel

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 ==Protein kinase A (PKA)==
-<StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''>
+<StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''>
 '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.
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 == Structure ==
-PKA consists of two types of subunits. It has a 49-kd regulatory <scene name='58/582909/Regulatory_subunits/1'>TextToBeDisplayed</scene>) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.
+PKA consists of two types of subunits. It has a 49-kd regulatory <scene name='58/582909/Regulatory_subunits/1'>regulatory subunit</scene>)(R) and a 38-kd <scene name='58/582909/Catalytic_subunits/1'>catalytic subunit</scene> (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.
 == Mechanism ==