Sandbox Reserved 694
From Proteopedia
| This Sandbox is Reserved from 30/01/2013, through 30/12/2013 for use in the course "Biochemistry II" taught by Hannah Tims at the Messiah College. This reservation includes Sandbox Reserved 686 through Sandbox Reserved 700. |
To get started:
More help: Help:Editing |
THE ANTHRAX PROTECTIVE ANTIGEN
|
by Matt Wier
Tetrameric Structure
The is a tetrameric protein that functions to bind to host receptors on the plasma membrane to translocate the anthrax toxin factors into the host cell. The PA must first form a heptamer with other PA's before it can bind to host receptors. The monomer form contains four domains that each serve unique functions. The contains a Furin cleavage site, the binding site for the toxin factors, and two Calcium ions (green) for stabilizaion. The contains a flexible loop to aid in plasma membrane insertion. The interacts with other PA's in the heptamer form. The is the most important domain because it can undergo a conformational change to allow heptamerization to occur.
