OspA L03 Group2: Difference between revisions
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<Structure load='1FJ1' size='400' align='left' caption='OspA' scene='OspA_L03_Group2/Default/1' /> | <Structure load='1FJ1' size='400' align='left' caption='OspA' scene='OspA_L03_Group2/Default/1' /> | ||
=== OspA === | |||
The model presented by the Protein Data Bank is OspA containing two [http://en.wikipedia.org/wiki/Immunoglobulin_light_chain light chains] or Hybridoma Antibody LA2 (chains A and C), two [http://en.wikipedia.org/wiki/Heavy_chain heavy chains] or Hyrbridoma Antibody LA2 (chains B and D), and two outer surface protein A (chains E and F). Model with Labeled Chains</scene> In addition, the original PDB image suggests that the C-terminal domain was unchanged by the LA-2 binding, other than minor shifts in the conformations of all 3-loops to accommodate interactions with the Fab <ref name=Ding >PMID: 11183781</ref>. | The model presented by the Protein Data Bank is OspA containing two [http://en.wikipedia.org/wiki/Immunoglobulin_light_chain light chains] or Hybridoma Antibody LA2 (chains A and C), two [http://en.wikipedia.org/wiki/Heavy_chain heavy chains] or Hyrbridoma Antibody LA2 (chains B and D), and two outer surface protein A (chains E and F). Model with Labeled Chains</scene> In addition, the original PDB image suggests that the C-terminal domain was unchanged by the LA-2 binding, other than minor shifts in the conformations of all 3-loops to accommodate interactions with the Fab <ref name=Ding >PMID: 11183781</ref>. | ||
<scene name='OspA_L03_Group2/Labeling_chains/1'>Chain Locations</scene> | <scene name='OspA_L03_Group2/Labeling_chains/1'>Chain Locations</scene> | ||
=== LA-2 === | |||
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 exposing the C-terminal to express the interaction with the Fab antigen combing site exposing the 3-loops where LA-2 makes direct contact <ref name=Ding >PMID: 11183781</ref>. | 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 exposing the C-terminal to express the interaction with the Fab antigen combing site exposing the 3-loops where LA-2 makes direct contact <ref name=Ding >PMID: 11183781</ref>. | ||
The following is the fit mechanism where the conformations recognize LA-2 and shifts to optimize the complementary antigen combing site (Ding, 2000). 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 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.<scene name='OspA_L03_Group2/Residues_203-220_loop1/2'>Residues 203 to 220 in "loop 1"</scene>” were represented by pale green, <scene name='OspA_L03_Group2/Residues_224-233_loop2/2'>residues 224-233 in loop 2</scene> were colored purple and <scene name='OspA_L03_Group2/Residues_246-257_loop3/3'>residues 247-257 in "loop 3"</scene>” 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_208/4'>Ala-208</scene> as | ==== Binding sites of OspA with LA-2 ==== | ||
The following is the fit mechanism where the conformations recognize LA-2 and shifts to optimize the complementary antigen combing site (Ding, 2000). 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 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.<scene name='OspA_L03_Group2/Residues_203-220_loop1/2'>Residues 203 to 220 in "loop 1"</scene>” were represented by pale green, <scene name='OspA_L03_Group2/Residues_224-233_loop2/2'>residues 224-233 in loop 2</scene> were colored purple and <scene name='OspA_L03_Group2/Residues_246-257_loop3/3'>residues 247-257 in "loop 3"</scene>” 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_208/4'>Ala-208</scene> as orange and <scene name='OspA_L03_Group2/Ala_215/4'>Ala-215</scene> as yellow 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)'''== | ||