Lei Jin coauthored structural research on how heparin activates the inhibitory protein antithrombin. A 1997 paper compared crystallographic structures involving active and latent antithrombin and its high-affinity five-sugar binding sequence at 2.9-ångström resolution.[ref]
The anticoagulant activation of antithrombin by heparin by Lei Jin and others. Original byline and Abstract; pentasaccharide-associated structures
The study linked binding to changes in the main beta sheet and exposure of the reactive-center loop, providing a structural account of how a carbohydrate ligand changes the behaviour of a serpin.[ref]
The anticoagulant activation of antithrombin by heparin by Lei Jin and others. Abstract; conformational changes associated with activation
The point is more informative than simply observing that heparin and antithrombin bind: the locations of structural changes suggest how binding can alter access to the inhibitory machinery. Articles by others on the same topic
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