Sandbox Reserved 1091: Difference between revisions

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The '''domain structure of ASP''' consists of the propeptide, the catalytic subtilisin-like domain, and the P-domain. The ASP molecule have two mean regions: an N-terminal region extending from Gly-3 to Pro-431 and forming the <scene name='82/829344/The_subtilisin_domain/2'>subtilisin domain</scene>, and a C-terminal region extending from Leu-432 to His-595 and forming the <scene name='82/829344/The_p-domain/2'>P-domain</scene>.

Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, ~~and~~ <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. It were assigned to ASP based on electron density, counter charges, and coordination. But in contrary to Kex2 ([[1r64]]), ASP ~~contains no~~ Ca2+ binding sites near its catalytic site.

Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, while <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. These findings were assigned to ASP based on electron density, counter charges, and coordination. But contrary to Kex2 ([[1r64]]), ASP doesn't contain any Ca2+ binding sites near its catalytic site.

A schematic representation of the domains of the protein can be observed : [http://www.degruyter.com/viewimg/j/bchm.2017.398.issue-10/hsz-2016-0344/hsz-2016-0344.xml?img=graphic/j_hsz-2016-0344_fig_001.jpg '''secondary structure of ASP''']. We can see that Kex2 has the propeptide (in yellow) that is absent in ASP. The occluding subdomains in the C-terminal region of ASP are shown in dark blue.

Sandbox Reserved 1091: Difference between revisions

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 The '''domain structure of ASP''' consists of the propeptide, the catalytic subtilisin-like domain, and the P-domain. The ASP molecule have two mean regions: an N-terminal region extending from Gly-3 to Pro-431 and forming the <scene name='82/829344/The_subtilisin_domain/2'>subtilisin domain</scene>, and a C-terminal region extending from Leu-432 to His-595 and forming the <scene name='82/829344/The_p-domain/2'>P-domain</scene>.
-Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, and <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. It were assigned to ASP based on electron density, counter charges, and coordination. But in contrary to Kex2 ([[1r64]]), ASP contains no Ca2+ binding sites near its catalytic site.
+Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, while <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. These findings were assigned to ASP based on electron density, counter charges, and coordination. But contrary to Kex2 ([[1r64]]), ASP doesn't contain any Ca2+ binding sites near its catalytic site.
 A schematic representation of the domains of the protein can be observed : [http://www.degruyter.com/viewimg/j/bchm.2017.398.issue-10/hsz-2016-0344/hsz-2016-0344.xml?img=graphic/j_hsz-2016-0344_fig_001.jpg '''secondary structure of ASP''']. We can see that Kex2 has the propeptide (in yellow) that is absent in ASP. The occluding subdomains in the C-terminal region of ASP are shown in dark blue.