The dimeric structure of factor XI and zymogen activation

Author:

Geng Yipeng1,Verhamme Ingrid M.1,Smith Stephen B.1,Sun Mao-fu1,Matafonov Anton1,Cheng Qiufang1,Smith Stephanie A.2,Morrissey James H.2,Gailani David13

Affiliation:

1. Department of Pathology, Microbiology, and Immunology, Vanderbilt University, Nashville, TN;

2. Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL; and

3. Department of Medicine, Vanderbilt University, Nashville, TN

Abstract

Key Points FXI must be a dimer for normal activation by fXIIa but not for activation by thrombin or autoactivation. Poly-P is a cofactor for activation of coagulation fXI by fXIIa and thrombin and supports fXI autoactivation.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Reference49 articles.

1. Structure and function of factor XI.;Emsley;Blood,2010

2. Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII.;Bouma;J Biol Chem,1977

3. Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein.;Fujikawa;Biochemistry,1986

4. Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.;McMullen;Biochemistry,1991

5. Crystal structure of the factor XI zymogen reveals a pathway for transactivation.;Papagrigoriou;Nat Struct Mol Biol,2006

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