your limit has been reached. plz Donate us to allow your ip full access, Email: sshnevis@outlook.com

Domain structure of coagulation factor XI and three-dimensional model of the factor XI dimer

Factor XI structure is shown:

A is the two-dimensional protein structure of a factor XI monomer. The four apple domains in the amino-terminal portion of the protein are labeled A1, A2, A3, and A4. The bond between Arg369 and Ile370 is in the lower part of the catalytic domain; cleavage of this bond by factor XIIa is important for factor XI activation.
B is a three-dimensional image of the factor XI homodimer. The white side chains represent Arg369 and Ile370 from the activation loop of the serine protease domain. The blue side chain represents Lys252 and Lys253, implicated in GpIb binding. The red side chain represents Glu66, a critical amino acid for thrombin binding (GpIb and thrombin binding are indicated by white arrows).

A1-4: apple domains; GpIb: platelet glycoprotein 1b.

(A) Adapted with permission from: McMullen BA, Fujikawa K, Davie EW. Location of the disulfide bonds in human coagulation factor XI: The presence of tandem apple domains. Biochemistry 1991; 30:2056. Copyright © 1991 American Chemical Society.
(B) Reprinted by permission from: Nature Publishing Group: Nature Structural and Molecular Biology. Papagrigoriou E, McEwan PA, Walsh PN, Emsley J. Crystal structure of the factor XI zymogen reveals a pathway for transactivation. Nat Struct Mol Biol 2006; 13:557. Copyright © 2006. https://www.nature.com/nsmb/.

Graphic 119188 Version 5.0