Sandbox Reserved 694
From Proteopedia
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== Tetrameric Structure == | == Tetrameric Structure == | ||
| - | 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 <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_2/1'>Domain 2</scene> contains a flexible loop to aid in plasma membrane insertion. The | + | 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 <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_2/1'>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 DOMAIN 4 is the most important domain because it can undergo a conformational change to allow heptamerization to occur. |
Revision as of 21:02, 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
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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 DOMAIN 4 is the most important domain because it can undergo a conformational change to allow heptamerization to occur.
