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 Blood, 15 February 2008, Vol. 111, No. 4, pp. 2049-2052.
Prepublished online as a Blood First Edition Paper on December 6, 2007; DOI 10.1182/blood-2007-09-114215.

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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY

Brief Report

X-ray crystal structure of the fibrinolysis inhibitor {alpha}2-antiplasmin

Ruby H. P. Law1, Trifina Sofian2, Wan-Ting Kan1,3, Anita J. Horvath2, Corinne R. Hitchen2, Christopher G. Langendorf1, Ashley M. Buckle1, James C. Whisstock1,3, and Paul B. Coughlin2

1 Department of Biochemistry and Molecular Biology, Monash University, Clayton; 2 Australian Centre for Blood Diseases, Monash University, Prahran; and 3 Australian Research Council (ARC) Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, Australia

The serpin {alpha}2-antiplasmin (SERPINF2) is the principal inhibitor of plasmin and inhibits fibrinolysis. Accordingly, {alpha}2-antiplasmin deficiency in humans results in uncontrolled fibrinolysis and a bleeding disorder. {alpha}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 2.65Å X-ray crystal structure of an N-terminal truncated murine {alpha}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 Center Loop where it may act as a template to accelerate serpin/protease interactions.


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