This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fie
From Proteopedia
RECOMBINANT HUMAN COAGULATION FACTOR XIII
Overview
The three-dimensional structure of the recombinant human factor XIII a2 dimer after cleavage by thrombin has been determined by X-ray crystallography. Factor XIII zymogen was treated with bovine alpha-thrombin in the presence of 3 mM CaCl2, and the cleaved protein was crystallized from Tris buffered at pH 6.5 using ethanol as the precipitating agent. Refinement of the molecular model of thrombin-cleaved factor XIII against diffraction data from 10.0 to 2.5 A resolution has been carried out to give a crystallographic R factor of 18.2%. The structure of thrombin-cleaved factor XIII is remarkably similar to that of the zymogen: there are no large conformational changes in the protein and the 37 residue amino terminus activation peptide remains associated with the rest of the molecule. This work shows that the activation peptide, upon thrombin cleavage, has the same conformation and occupies the same position with respect to the rest of the molecule as it does in the zymogen structure.
About this Structure
1FIE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII., Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC, Thromb Res. 1995 Jun 1;78(5):389-97. PMID:7660355 Page seeded by OCA on Fri May 2 16:21:57 2008
