1ggt
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(New page: 200px<br /> <applet load="1ggt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggt, resolution 2.65Å" /> '''THREE-DIMENSIONAL S...)
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Revision as of 14:58, 12 November 2007
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THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII
Contents |
Overview
Mechanical stability in many biological materials is provided by the, crosslinking of large structural proteins with, gamma-glutamyl-epsilon-lysyl amide bonds. The three-dimensional structure, of human recombinant factor XIII (EC 2.3.2.13 zymogen;, protein-glutamine:amine gamma-glutamyltransferase a chain), a, transglutaminase zymogen, has been solved at 2.8-A resolution by x-ray, crystallography. This structure shows that each chain of the homodimeric, protein is folded into four sequential domains. A catalytic triad, reminiscent of that observed in cysteine proteases has been identified in, the core domain. The amino-terminal activation peptide of each subunit, crosses the dimer interface and partially occludes the opening of the, catalytic cavity in the second subunit, preventing substrate binding to, the zymogen. A proposal for the mechanism of activation by thrombin and, calcium is made that details the structural events leading to active, factor XIIIa'.
Disease
Known disease associated with this structure: Factor XIIIA deficiency OMIM:[134570]
About this Structure
1GGT is a Single protein structure of sequence from Homo sapiens. Active as Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII., Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC, Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7296-300. PMID:7913750
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