User:Yunlong Zhao/Sandbox 1: Difference between revisions

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== The allosteric mechanism of heparin-based anticoagulant activation ==

A model of anticoagulant activation of antithrombin by heparin was described as an allosteric mechanism. In another word, heparin chain binds to antithrombin and stabilizes the inhibitory conformation (the inhibitory loop is outward) or alters the antithrombin conformation to facilitate the antithrombin-protease interaction. Early published crystal structure of pentasaccharide-bond antithrombin provided many details of the interaction and validated this hypothesis to some extents. Pentasaccharide binds to the <scene name='58/584311/Binding_helices/2'>~~helix~~ region</scene> distal to the inhibitory loop.

A model of anticoagulant activation of antithrombin by heparin was described as an allosteric mechanism. In another word, heparin chain binds to antithrombin and stabilizes the inhibitory conformation (the inhibitory loop is outward) or alters the antithrombin conformation to facilitate the antithrombin-protease interaction. Early published crystal structure of pentasaccharide-bond antithrombin provided many details of the interaction and validated this hypothesis to some extents. Pentasaccharide binds to the <scene name='58/584311/Binding_helices/3'>helical region</scene> distal to the inhibitory loop.

Green scene 2 will be the the interface structure plus heparin

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 == The allosteric mechanism of heparin-based anticoagulant activation ==
-A model of anticoagulant activation of antithrombin by heparin was described as an allosteric mechanism. In another word, heparin chain binds to antithrombin and stabilizes the inhibitory conformation (the inhibitory loop is outward) or alters the antithrombin conformation to facilitate the antithrombin-protease interaction. Early published crystal structure of pentasaccharide-bond antithrombin provided many details of the interaction and validated this hypothesis to some extents. Pentasaccharide binds to the <scene name='58/584311/Binding_helices/2'>helix region</scene> distal to the inhibitory loop.
+A model of anticoagulant activation of antithrombin by heparin was described as an allosteric mechanism. In another word, heparin chain binds to antithrombin and stabilizes the inhibitory conformation (the inhibitory loop is outward) or alters the antithrombin conformation to facilitate the antithrombin-protease interaction. Early published crystal structure of pentasaccharide-bond antithrombin provided many details of the interaction and validated this hypothesis to some extents. Pentasaccharide binds to the <scene name='58/584311/Binding_helices/3'>helical region</scene> distal to the inhibitory loop.
 Green scene 2 will be the the interface structure plus heparin