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[[Image:1fie.gif|left|200px]]<br />
<applet load="1fie" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fie, resolution 2.5&Aring;" />
'''RECOMBINANT HUMAN COAGULATION FACTOR XIII'''<br />


==Overview==
==RECOMBINANT HUMAN COAGULATION FACTOR XIII==
The three-dimensional structure of the recombinant human factor XIII a2, dimer after cleavage by thrombin has been determined by X-ray, crystallography. Factor XIII zymogen was treated with bovine, alpha-thrombin in the presence of 3 mM CaCl2, and the cleaved protein was, crystallized from Tris buffered at pH 6.5 using ethanol as the, precipitating agent. Refinement of the molecular model of thrombin-cleaved, factor XIII against diffraction data from 10.0 to 2.5 A resolution has, been carried out to give a crystallographic R factor of 18.2%. The, structure of thrombin-cleaved factor XIII is remarkably similar to that of, the zymogen: there are no large conformational changes in the protein and, the 37 residue amino terminus activation peptide remains associated with, the rest of the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?7660355 (full description)]]
<StructureSection load='1fie' size='340' side='right'caption='[[1fie]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fie]] 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=1FIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FIE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=1fie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fie OCA], [https://pdbe.org/1fie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fie RCSB], [https://www.ebi.ac.uk/pdbsum/1fie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fie ProSAT]</span></td></tr>
</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/fi/1fie_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=1fie ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FIE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[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]]. Structure known Active Sites: CAT and CBT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FIE OCA]].
*[[Factor XIII|Factor XIII]]
 
== References ==
==Reference==
<references/>
Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII., Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC, Thromb Res. 1995 Jun 1;78(5):389-97. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7660355 7660355]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-glutamine gamma-glutamyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Teller DC]]
[[Category: Teller, D.C.]]
[[Category: Yee VC]]
[[Category: Yee, V.C.]]
[[Category: acyltransferase]]
[[Category: blood coagulation]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:36:30 2007''
Retrieved from "https://proteopedia.org/1fie"