1ggt: Difference between revisions

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[[Image:1ggt.gif|left|200px]]


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==THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII==
The line below this paragraph, containing "STRUCTURE_1ggt", creates the "Structure Box" on the page.
<StructureSection load='1ggt' size='340' side='right'caption='[[1ggt]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ggt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GGT FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
-->
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ggt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggt OCA], [https://pdbe.org/1ggt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ggt RCSB], [https://www.ebi.ac.uk/pdbsum/1ggt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ggt ProSAT]</span></td></tr>
{{STRUCTURE_1ggt| PDB=1ggt |  SCENE= }}
</table>
== Disease ==
[https://www.uniprot.org/uniprot/F13A_HUMAN F13A_HUMAN] Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [MIM:[https://omim.org/entry/613225 613225]. FA13AD is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.<ref>PMID:1353995</ref>
== Function ==
[https://www.uniprot.org/uniprot/F13A_HUMAN F13A_HUMAN] Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/1ggt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ggt ConSurf].
<div style="clear:both"></div>


'''THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII'''
==See Also==
 
*[[Factor XIII|Factor XIII]]
 
== References ==
==Overview==
<references/>
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'.
__TOC__
 
</StructureSection>
==About this Structure==
1GGT 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=1GGT 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:[http://www.ncbi.nlm.nih.gov/pubmed/7913750 7913750]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-glutamine gamma-glutamyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Bishop PD]]
[[Category: Bishop, P D.]]
[[Category: Pedersen LC]]
[[Category: Pedersen, L C.]]
[[Category: Stenkamp RE]]
[[Category: Stenkamp, R E.]]
[[Category: Teller DC]]
[[Category: Teller, D C.]]
[[Category: Trong IL]]
[[Category: Trong, I L.]]
[[Category: Yee VC]]
[[Category: Yee, V C.]]
[[Category: Blood coagulation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:32:33 2008''

Latest revision as of 07:25, 7 February 2024

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

1ggt, resolution 2.65Å

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