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> 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 monomer form contains <scene name='Sandbox_Reserved_694/4_colored_domains/1'>four domains</scene> that each serve unique functions. The <scene name='Sandbox_Reserved_694/Domain_1/2'>Domain 1</scene> contains a Furin cleavage site, the binding site for the toxin factors, and two Calcium ions (green) for stabilizaion. The <scene name='Sandbox_Reserved_694/Domain_2/2'>Domain 2</scene> contains a flexible loop to aid in plasma membrane insertion. The <scene name='Sandbox_Reserved_694/Domain_3/1'>Domain 3</scene> interacts with other PA's in the heptamer form. The <scene name='Sandbox_Reserved_694/Domain_4/1'>Domain 4</scene> is the most important domain because it can undergo a conformational change to allow heptamerization to occur. Monomer PA's must oligomerize to form a heptamer before it can bind to host receptors and translocate the toxin into the cell.
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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 monomer form contains <scene name='Sandbox_Reserved_694/4_colored_domains/1'>four domains</scene> that each serve unique functions. The <scene name='Sandbox_Reserved_694/Domain_1/3'>Domain 1</scene> contains a Furin cleavage site, the binding site for the toxin factors, and two Calcium ions (green) for stabilizaion. The <scene name='Sandbox_Reserved_694/Domain_2/2'>Domain 2</scene> contains a flexible loop to aid in plasma membrane insertion. The <scene name='Sandbox_Reserved_694/Domain_3/1'>Domain 3</scene> interacts with other PA's in the heptamer form. The <scene name='Sandbox_Reserved_694/Domain_4/1'>Domain 4</scene> is the most important domain because it can undergo a conformational change to allow heptamerization to occur. Monomer PA's must oligomerize to form a heptamer before it can bind to host receptors and translocate the toxin into the cell.

Revision as of 21:23, 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 monomer form contains 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. Monomer PA's must oligomerize to form a heptamer before it can bind to host receptors and translocate the toxin into the cell.

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