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Sandbox Reserved 694

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== Tetrameric Structure ==
== Tetrameric Structure ==
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The <scene name='Sandbox_Reserved_694/Normal_pa/1'>anthrax protective antigen (PA)</scene> contains four domains that are crucial for its functionality. The first
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The <scene name='Sandbox_Reserved_694/Normal_pa/1'>anthrax protective antigen (PA)</scene> 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 DOMAIN 1 contains a Furin cleavage site and the binding site for the toxin factors. The DOMAIN 2 contains a flexible loop to aid in plasma membrane insertion. The DOMAIN 3 interacts with other PA's in the heptamer form. The DOMAIN 4 is the most important domain because it can undergo a conformational change to allow heptamerization to occur.

Revision as of 20:32, 27 April 2013

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.
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THE ANTHRAX PROTECTIVE ANTIGEN

Anthrax protective antigen complex (blue) with stabilizing Ca2+ (green) (PDB ID: 1ACC)

Drag the structure with the mouse to rotate

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 DOMAIN 1 contains a Furin cleavage site and the binding site for the toxin factors. The DOMAIN 2 contains a flexible loop to aid in plasma membrane insertion. The DOMAIN 3 interacts with other PA's in the heptamer form. The DOMAIN 4 is the most important domain because it can undergo a conformational change to allow heptamerization to occur.

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