1ggt: Difference between revisions

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[[Image:1ggt.gif|left|200px]]
{{Seed}}
[[Image:1ggt.png|left|200px]]


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{{STRUCTURE_1ggt|  PDB=1ggt  |  SCENE=  }}  
{{STRUCTURE_1ggt|  PDB=1ggt  |  SCENE=  }}  


'''THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII'''
===THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII===




==Overview==
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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'.
The line below this paragraph, {{ABSTRACT_PUBMED_7913750}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7913750 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7913750}}


==About this Structure==
==About this Structure==
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[[Category: Yee, V C.]]
[[Category: Yee, V C.]]
[[Category: Blood coagulation]]
[[Category: Blood coagulation]]
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