PDBsum entry 1ggt

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Blood coagulation PDB id
Protein chain
710 a.a. *
* Residue conservation analysis

References listed in PDB file
Key reference
Title Three-Dimensional structure of a transglutaminase: human blood coagulation factor xiii.
Authors V.C.Yee, L.C.Pedersen, I.Le trong, P.D.Bishop, R.E.Stenkamp, D.C.Teller.
Ref. Proc Natl Acad Sci U S A, 1994, 91, 7296-7300. [DOI no: 10.1073/pnas.91.15.7296]
PubMed id 7913750
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 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'.
Secondary reference #1
Title The catalytic triad and proposed mechanism of transglutaminases based on the crystal structure of factor xiii
Authors L.C.Pedersen, V.C.Yee, I.L.Trong, P.D.Bishop, D.C.Teller, R.E.Stenkamp.
Ref. protein sci., 1994, 3, 1131.
Secondary reference #2
Title Human recombinant factor xiii from saccharomyces cerevisiae: crystallization and preliminary x-Ray data
Authors P.D.Bishop, G.W.Lasser, I.L.Trong, R.E.Stenkamp, D.C.Teller.
Ref. j.biol.chem., 1990, 23, 13888.
Secondary reference #3
Title Human recombinant factor xiii from saccharomyces cerevisiae. Crystallization and preliminary x-Ray data.
Authors P.D.Bishop, G.W.Lasser, I.Le trong, R.E.Stenkamp, D.C.Teller.
Ref. J Biol Chem, 1990, 265, 13888-13889.
PubMed id 2199445
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