OspA L03 Group2: Difference between revisions
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The reactive LA-2 antibody was found to serve as an important epitope of Osp-A binding <ref name=Ding >PMID: 11183781</ref> towards developing vaccinations. The protein, OspA obtained from PDB was dissected to isolate and concentrate the F chain from the molecule of OspA from the crystallized structure to show the free state of the 3D model exposed the C-terminal. | The reactive LA-2 antibody was found to serve as an important epitope of Osp-A binding <ref name=Ding >PMID: 11183781</ref> towards developing vaccinations. The protein, OspA obtained from PDB was dissected to isolate and concentrate the F chain from the molecule of OspA from the crystallized structure to show the free state of the 3D model exposed the C-terminal. | ||
There were 49 residues from the “three loops” involved that significantly affected by LA-2 binding, through findings from NMR and crystallization <ref name=Ding >PMID: 11183781</ref>. Residues 207 and 227 from “loop 1” were excluded from analysis because of the peak overlap <ref name=Ding >PMID: 11183781</ref>. The portion of the protein chain detected through 15N-HSQC NMR that were affected by the binding of LA2 <ref name=Ding >PMID: 11183781</ref> was highlighted.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 <scene name='OspA_L03_Group2/Ala_215/1'>Ala215</scene> 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 <ref name=Ding >PMID: 11183781</ref>. | There were 49 residues from the “three loops” involved that significantly affected by LA-2 binding, through findings from NMR and crystallization <ref name=Ding >PMID: 11183781</ref>. Residues 207 and 227 from “loop 1” were excluded from analysis because of the peak overlap <ref name=Ding >PMID: 11183781</ref>. The portion of the protein chain detected through 15N-HSQC NMR that were affected by the binding of LA2 <ref name=Ding >PMID: 11183781</ref> was highlighted.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 <scene name='OspA_L03_Group2/Ala_208/1'>Ala208</scene> as red and <scene name='OspA_L03_Group2/Ala_215/1'>Ala215</scene> 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 <ref name=Ding >PMID: 11183781</ref>. | ||
=='''Vaccination (La-2)'''== | =='''Vaccination (La-2)'''== | ||