Protein Kinase A

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This is a default text for your page Protein Kinase A. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function Protein Kinase A (PKA) helps animals cope with stressful situations. In the "flight or fight" response, muscle becomes primed for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. (? makes sure this is right) Structure PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) 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+. Structural highlights This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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ReferencesReferences

[1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644 [2]C. Kim, N.-H. Xuong, and S.S. Taylor, "Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,"Science 307, 690 (2005)