1fie
From Proteopedia
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| - | [[Image:1fie.gif|left|200px]] | + | [[Image:1fie.gif|left|200px]] |
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| - | '''RECOMBINANT HUMAN COAGULATION FACTOR XIII''' | + | {{Structure |
| + | |PDB= 1fie |SIZE=350|CAPTION= <scene name='initialview01'>1fie</scene>, resolution 2.5Å | ||
| + | |SITE= <scene name='pdbsite=CAT:Active+Site,+Catalytic+Triad'>CAT</scene> and <scene name='pdbsite=CBT:Active+Site,+Catalytic+Triad'>CBT</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''RECOMBINANT HUMAN COAGULATION FACTOR XIII''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FIE is a [ | + | 1FIE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIE OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7660355 7660355] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-glutamine gamma-glutamyltransferase]] | [[Category: Protein-glutamine gamma-glutamyltransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:35 2008'' |
Revision as of 09:09, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Activity: | Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RECOMBINANT HUMAN COAGULATION FACTOR XIII
Contents |
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.
Disease
Known disease associated with this structure: Factor XIIIA deficiency OMIM:[134570]
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 Thu Mar 20 11:09:35 2008
