1fie
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RECOMBINANT HUMAN COAGULATION FACTOR XIII
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1FIE is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Protein-glutamine gamma-glutamyltransferase], with EC number [2.3.2.13]. Structure known Active Sites: CAT and CBT. Full crystallographic information is available from [OCA].
ReferenceReference
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
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