X-ray crystal structure of the fibrinolysis inhibitor alpha2-antiplasmin

Ruby Hong Ping Law, Trifina Sofian, Wan-Ting Kan, Anita Julieanne Horvath, Corinne Raylene Hitchen, Christopher Langendorf, Ashley Maurice Buckle, James Whisstock, Paul Bernard Coughlin

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29 Citations (Scopus)


The serpin 2-antiplasmin (SERPINF2) is the principal inhibitor of plasmin and inhibits fibrinolysis. Accordingly, 2-antiplasmin deficiency in humans results in uncontrolled fibrinolysis and a bleeding disorder. 2-antiplasmin is an unusual serpin, in that it contains extensive N- and C-terminal sequences flanking the serpin domain. The N-terminal sequence is crosslinked to fibrin by factor XIIIa, whereas the C-terminal region mediates the initial interaction with plasmin. To understand how this may happen, we have determined the 2.65 ? X-ray crystal structure of an N-terminal truncated murine 2-antiplasmin. The structure reveals that part of the C-terminal sequence is tightly associated with the body of the serpin. This would be anticipated to position the flexible plasmin-binding portion of the C-terminus in close proximity to the serpin Reactive Centre Loop where it may template serpin / protease interactions.
Original languageEnglish
Pages (from-to)2049 - 2052
Number of pages3
Publication statusPublished - 2008

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