Sandbox 1k4r: Difference between revisions
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<StructureSection load='1ok8' size='500' side='right' caption='Dengue virus inside cell (PDB entry [[1ok8]])' scene=''> | <StructureSection load='1ok8' size='500' side='right' caption='Dengue virus inside cell (PDB entry [[1ok8]])' scene=''> | ||
'''Dengue Virus inside Cell''' ([[1ok8]]) | '''Dengue Virus inside Cell''' ([[1ok8]]) | ||
When the virus is in its infectious form the surface is smooth (''figure 1''), but as it is exposed to the acidic environment of the cell causes the proteins to snap into a trimeric spike (or trimer, which allows it to penetrate and fuse with the lysozome membrane of the host cell. | When the virus is in its infectious form the surface is smooth (''figure 1''), but as it is exposed to the acidic environment of the cell cytoplasm, this causes the proteins to snap into a trimeric spike (or trimer), which allows it to penetrate and fuse with the lysozome membrane of the host cell. | ||
In experimental laboratory settings, the extraction of this trimer model can be done in many different ways. The main, observed, extraction was separated by detergent isolation. The model shows a chloride ion (detergent) liganded by three amide nitrogens from Lys-110. The chloride is believed to dissolve away the liposome on the trimer tip. The tip of the trimer, or <scene name='56/565763/Trimer/3'>fusion loop</scene>, displays three hydrophobic residues, Trp-101, Lys-107, and Phe-108. | In experimental laboratory settings, the extraction or isolation of this trimer model can be done in many different ways. The main, observed, extraction was separated by detergent isolation. The model shows a chloride ion (detergent) liganded by three amide nitrogens from Lys-110. The chloride is believed to dissolve away the liposome on the trimer tip. The tip of the trimer, or <scene name='56/565763/Trimer/3'>fusion loop</scene>, displays three hydrophobic residues, Trp-101, Lys-107, and Phe-108. | ||
Due to this dissolution from the chloride molecule, the three-fold –clustered membrane tip does not tightly bind together and thereby does not penetrate very deep into the host cell membrane. The fusion loop is thinking to be held into the membrane by an “aromatic anchor” formed by Trp-101 and Phe-108 | Due to this dissolution from the chloride molecule, the three-fold –clustered membrane tip does not tightly bind together and thereby does not penetrate very deep into the host cell membrane. The fusion loop is thinking to be held into the membrane by an “aromatic anchor” formed by Trp-101 and Phe-108 | ||
</StructureSection> | </StructureSection> | ||