Sandbox Reserved 960: Difference between revisions

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== Structure ==
== Structure ==
[[Image: 3fe6_cartoon.jpg|250px|left|thumb|'''Fig.1''' Ribbon colored representation]]


ASP1 is composed of <scene name='60/604479/Helixes/1'>7 right-handed alpha helixes</scene>  (<scene name='60/604479/H1/2'>H1</scene>, residues 8–25; <scene name='60/604479/H2/2'>H2</scene>, residues 27–36; <scene name='60/604479/H3/2'>H3</scene>, residues 42–56; <scene name='60/604479/H4/1'>H4</scene>, residues 66–74 ; <scene name='60/604479/H5/1'>H5</scene>, residues 75–77 ; <scene name='60/604479/H6/1'>H6</scene>,residues 78–90 ;<scene name='60/604479/H7/1'>H7</scene>, residues 96–112)  
ASP1 is composed of <scene name='60/604479/Helixes/1'>7 right-handed alpha helixes</scene>  (<scene name='60/604479/H1/2'>H1</scene>, residues 8–25; <scene name='60/604479/H2/2'>H2</scene>, residues 27–36; <scene name='60/604479/H3/2'>H3</scene>, residues 42–56; <scene name='60/604479/H4/1'>H4</scene>, residues 66–74 ; <scene name='60/604479/H5/1'>H5</scene>, residues 75–77 ; <scene name='60/604479/H6/1'>H6</scene>,residues 78–90 ;<scene name='60/604479/H7/1'>H7</scene>, residues 96–112)  


Helix 1 has a break in the hydrogen-bonding pattern of its structure, forming tight substitute hydrogen bonds with water molecules. Indeed, it results in a kink in helix 1 (at residue Ala 14)(scene) induced by a disruption in the helical conformation, due to hydrogen bonds with water molecules.
<scene name='60/604479/H1/2'>H1</scene> has a break in the hydrogen-bonding pattern of its structure, forming tight substitute hydrogen bonds with water molecules. Thus, it results in a kink (at residue Ala 14)(scene) induced by a disruption in the helical conformation, due to hydrogen bonds with water molecules.


The C terminal(scene) domain of this molecule presents a characteristic PBP-GOP domain. While this protein is composed of 144 residues the domain PBP begin at 25 residue. ASP1 binds its ligand at low pH and releases it at neutral pH.
The C terminal(scene) domain of this molecule presents a characteristic PBP-GOP domain. While this protein is composed of 144 residues the domain PBP begin at 25 residue. ASP1 binds its ligand at low pH and releases it at neutral pH.
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=== Components implicated in the structure rigidity: ===
=== Components implicated in the structure rigidity: ===
ASP1 presents three disulfides bridges which are greatly enhancing its structure’s rigidity by linking four of the helixes together (scene).  
ASP1 presents <scene name='60/604479/Disulfide_bonds/1'> three disulfide bridges</scene> which are greatly enhancing its structure’s rigidity by linking four of the helixes together.  


The first disulfide bridge (scene) is established between H1 and H3 through Cysteins 20 and 51. An other disulfide bridge (scene) links H3 and H6 through Cys 47 and 98, and the third and last bridge (scene)connects H5 and H6 thanks to Cys 89 and Cys 107.  
The <scene name='60/604479/1st_disulfide_bridge/1'>first disulfide bridge</scene> is established between <scene name='60/604479/H1/2'>H1</scene> and <scene name='60/604479/H3/2'>H3</scene> through Cysteins 20 and 51. <scene name='60/604479/2nd_disulfide_bridge/1'>An other disulfide bridge</scene> (scene) links <scene name='60/604479/H3/2'>H3</scene> and <scene name='60/604479/H6/1'>H6</scene> through Cys 47 and 98, and the <scene name='60/604479/3rd_disulfide_bridge/1'>third disulfide bridge</scene> connects <scene name='60/604479/H5/1'>H5</scene> and <scene name='60/604479/H6/1'>H6</scene> thanks to Cys 89 and Cys 107.  


Furthermore, non covalent bonds also play an important role.   
Furthermore, non covalent bonds also play an important role.   
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