Protein Kinase A

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 ^[1] or to the article describing Jmol ^[2] 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.

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+.

Mechanism

Regulation

Disease

Relevance

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.