G09SecL04Tpc2: Difference between revisions

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=== LA-2 Recognition ===  
=== LA-2 Recognition ===  
<Structure load='1fj1' size='300' frame='true' align='right' caption='OspA and LA-2 Fab Complex' scene='G09SecL04Tpc2/Ospala2/1' />
<Structure load='1fj1' size='300' frame='true' align='right' caption='OspA and LA-2 Fab Complex' scene='G09SecL04Tpc2/Ospala2/1' />
<scene name='G09SecL04Tpc2/Ospala2/1'>Reset Model</scene>
 
Since NMR chemical shifts are greatly sensitive to magnetic (local) environments, they are great for sensing conformational changes; NMR chemical-shift perturbation was an important method in identifying this three- loop epitope of OspA, but more importantly it also portrayed that these three loops were strongly antigenic.  In a study conducted in 2000, Wei Ding and fellow colleagues illustrated the <scene name='G09SecL04Tpc2/Ospala2/2'>Binding Site</scene> through NMR and crystallography: LA-2 makes a concave-like groove over the 3 loops on the tip of the c-terminus through direct contact by heavy and light chains includng interactions between its R groups.  
Since NMR chemical shifts are greatly sensitive to magnetic (local) environments, they are great for sensing conformational changes; NMR chemical-shift perturbation was an important method in identifying this three- loop epitope of OspA, but more importantly it also portrayed that these three loops were strongly antigenic.  In a study conducted in 2000, Wei Ding and fellow colleagues illustrated the <scene name='G09SecL04Tpc2/Ospala2/2'>binding Site</scene> through NMR and crystallography: LA-2 makes a concave-like groove over the 3 loops on the tip of the c-terminus through direct contact by heavy and light chains includng interactions between its R groups.  


Subsequent NMR results suggested that the overall c-terminal was basically unchanged by LA-2 binding, except for the minor shifts in the conformations of the 3 loops; the conformations results in order to accommodate interactions witht Fab. Further analysis of amide proton exchange rates supported this by proving that the n-terminal and central sheet domains were stable while the c-terminal domain illustrated great fluctuation in respect to its 3 loops. Specifically, Loops 2 and 3 were only subject to slight change in comparison to Loop 1’s dramatic increase.
Subsequent NMR results suggested that the overall c-terminal was basically unchanged by LA-2 binding, except for the minor shifts in the conformations of the 3 loops; the conformations results in order to accommodate interactions witht Fab. Further analysis of amide proton exchange rates supported this by proving that the n-terminal and central sheet domains were stable while the c-terminal domain illustrated great fluctuation in respect to its 3 loops. Specifically, Loops 2 and 3 were only subject to slight change in comparison to Loop 1’s dramatic increase.