2R9Y

Structure of antiplasmin

Summary for 2R9Y

• Entry DOI: 10.2210/pdb2r9y/pdb
• Descriptor: Alpha-2-antiplasmin (2 entities in total)
• Functional Keywords: alpha2-antiplasmin, inhibitory serpin, plasmin inhibitor, acute phase, glycoprotein, protease inhibitor, secreted, serine protease inhibitor, sulfation, toxin, hydrolase inhibitor
• Biological source: Mus musculus (house mouse)
• Cellular location: Secreted: Q61247
• Total number of polymer chains: 1
• Total formula weight: 48611.16

Authors

Law, R.H.P.,Sofian, T.,Kan, W.T.,Horvath, A.J.,Hitchen, C.R.,Langendorf, C.G.,Buckle, A.M.,Whisstock, J.C.,Coughlin, P.B. (deposition date: 2007-09-14, release date: 2007-12-18, Last modification date: 2023-10-25)

Primary citation

Law, R.H.P.,Sofian, T.,Kan, W.T.,Horvath, A.J.,Hitchen, C.R.,Langendorf, C.G.,Buckle, A.M.,Whisstock, J.C.,Coughlin, P.B.
X-ray crystal structure of the fibrinolysis inhibitor {alpha}2-antiplasmin
Blood, 111:2049-2052, 2008

PubMed Abstract: 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 2.65A 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.

PubMed: 18063751
DOI: 10.1182/blood-2007-09-114215

Experimental method

X-RAY DIFFRACTION (2.65 Å)