User:Yunlong Zhao/Sandbox 1: Difference between revisions

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== Structure features and activation of latent antithrombin ==

Antithrombin is a natural inhibitor of many serine proteases and it contains an exposed inhibitory loop to intrude the catalytic site of proteases. The peptide bond between R393-S394 (shown as the sphere model in figure 1) plays a critical role in the inhibitory binding. However, the exposure of the inhibitory loop requires a conformational change during activation. In the latent state of antithrombin, this loop is fully buried in the four-strands beta sheet to form a new five-strands beta sheet. This remarkable conformational change of inhibitory loop highlights the activation mechanism of latent antithrombin. The figure below shows the process of the activation of antithrombin.[[Image:Activation_of_AT-III.png]~~Figure 1~~]

Antithrombin is a natural inhibitor of many serine proteases and it contains an exposed inhibitory loop to intrude the catalytic site of proteases. The peptide bond between R393-S394 (shown as the sphere model in figure 1) plays a critical role in the inhibitory binding. However, the exposure of the inhibitory loop requires a conformational change during activation. In the latent state of antithrombin, this loop is fully buried in the four-strands beta sheet to form a new five-strands beta sheet. This remarkable conformational change of inhibitory loop highlights the activation mechanism of latent antithrombin. The figure below shows the process of the activation of antithrombin.[[Image:Activation_of_AT-III.png]]

== The mechanism of heparin regulating antithrombin thrombin interaction ==

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 == Structure features and activation of latent antithrombin ==
-Antithrombin is a natural inhibitor of many serine proteases and it contains an exposed inhibitory loop to intrude the catalytic site of proteases. The peptide bond between R393-S394 (shown as the sphere model in figure 1) plays a critical role in the inhibitory binding. However, the exposure of the inhibitory loop requires a conformational change during activation. In the latent state of antithrombin, this loop is fully buried in the four-strands beta sheet to form a new five-strands beta sheet. This remarkable conformational change of inhibitory loop highlights the activation mechanism of latent antithrombin. The figure below shows the process of the activation of antithrombin.[[Image:Activation_of_AT-III.png]Figure 1]
+Antithrombin is a natural inhibitor of many serine proteases and it contains an exposed inhibitory loop to intrude the catalytic site of proteases. The peptide bond between R393-S394 (shown as the sphere model in figure 1) plays a critical role in the inhibitory binding. However, the exposure of the inhibitory loop requires a conformational change during activation. In the latent state of antithrombin, this loop is fully buried in the four-strands beta sheet to form a new five-strands beta sheet. This remarkable conformational change of inhibitory loop highlights the activation mechanism of latent antithrombin. The figure below shows the process of the activation of antithrombin.[[Image:Activation_of_AT-III.png]]
 == The mechanism of heparin regulating antithrombin thrombin interaction ==