Sandbox Reserved 960: Difference between revisions
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<StructureSection load='3fe6' size='400' side='right' | <StructureSection load='3fe6' size='400' side='right' | ||
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
<nowiki> | <nowiki> | ||
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=== Location in the antenna and transport of pheromones === | === Location in the antenna and transport of pheromones === | ||
== Structure == | == Structure == | ||
[[Image: 3fe6_cartoon.jpg|250px|left|thumb|'''Fig.1''' Ribbon colored representation]] | [[Image: 3fe6_cartoon.jpg|250px|left|thumb|'''Fig.1''' Ribbon colored representation]] | ||
=== Domains and family === | === Domains and family === | ||
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 the 25th residue. AmelASP1 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 the 25th residue. AmelASP1 binds its ligand at low pH and releases it at neutral pH. | ||
=== Key residues === | === Key residues === | ||
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<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 <scene name='60/604479/Kink/1'>kink</scene> (at residue Ala 14) 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 <scene name='60/604479/Kink/1'>kink</scene> (at residue Ala 14) induced by a disruption in the helical conformation, due to hydrogen bonds with water molecules. | ||
=== Components implicated in the structure rigidity === | === Components implicated in the structure rigidity === | ||
AmelASP1 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 helices together. The six cysteines and their interval spacing are the most striking features shared by proteins belonging to the PBP family. | AmelASP1 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 helices together. The six cysteines and their interval spacing are the most striking features shared by proteins belonging to the PBP family. | ||
