This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox Reserved 694
From Proteopedia
(→Tetrameric Structure) |
(→Tetrameric Structure) |
||
| Line 8: | Line 8: | ||
== 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/ | + | 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 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 20:48, 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. |
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 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.
