OspA L03 Group2: Difference between revisions
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=='''Structure'''== | =='''Structure'''== | ||
The reactive LA-2 antibody was found to serve as an important epitope of Osp-A binding (Ding, 2000) towards developing vaccinations. The protein obtained from PDB was dissected to isolate and concentrate the F chain from the molecule of OspA from the crystallized structure, since the structure was symmetric. The free state of the 3D model exposed the C-terminal where there were 49 residues from the “three loops” involved that significantly affected by LA-2 binding, through findings from NMR and crystallization (Ding, 2000). Residues 207 and 227 from “loop 1” were excluded from analysis because of the peak overlap (Ding, 2000). Residues 203 to 220 in “loop1” were represented by pale green, residues 224 to 233 in “loop 2” were colored purple and residues 246 to 257 in “loop 3” were colored medium slate blue. The cool coloring of the residues shows the location of LA-2’s direct contact on the “3 loops”. Primary colors were used to represent Ala208 as red and Ala215 as blue in spacefills for the primary or initial identification of the LA-2 epitope on the beta-strands. The coloration of resides are all at one end, C-terminal of the isolated OspA molecule showing the side where LA-2 binds. The rest of the model were beta-sheets that were left yellow, as the neutral color, and the only alpha-helix was colored pink, to show the general overall structure of 21 anti-parrallel beta-strands to 1 alpha-helix (Ding, 2000). | |||
=='''Vaccination (La-2)'''== | =='''Vaccination (La-2)'''== | ||
