1ggt

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[[Image:1ggt.gif|left|200px]]
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{{Structure
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|PDB= 1ggt |SIZE=350|CAPTION= <scene name='initialview01'>1ggt</scene>, resolution 2.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1ggt", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1ggt| PDB=1ggt | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ggt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggt OCA], [http://www.ebi.ac.uk/pdbsum/1ggt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ggt RCSB]</span>
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'''THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII'''
'''THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII'''
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[[Category: Trong, I L.]]
[[Category: Trong, I L.]]
[[Category: Yee, V C.]]
[[Category: Yee, V C.]]
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[[Category: blood coagulation]]
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[[Category: Blood coagulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:32:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:43:39 2008''
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Revision as of 14:32, 2 May 2008

Template:STRUCTURE 1ggt

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


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'.

About this Structure

1GGT is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Fri May 2 17:32:33 2008

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