1fie

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(New page: 200px<br /> <applet load="1fie" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fie, resolution 2.5&Aring;" /> '''RECOMBINANT HUMAN CO...)
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[[Image:1fie.gif|left|200px]]<br />
 
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<applet load="1fie" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fie, resolution 2.5&Aring;" />
 
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'''RECOMBINANT HUMAN COAGULATION FACTOR XIII'''<br />
 
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==Overview==
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==RECOMBINANT HUMAN COAGULATION FACTOR XIII==
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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)]]
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<StructureSection load='1fie' size='340' side='right'caption='[[1fie]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Disease ==
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[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>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/1fie_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FIE OCA]].
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*[[Factor XIII|Factor XIII]]
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== References ==
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==Reference==
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<references/>
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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]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Teller, D.C.]]
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[[Category: Teller DC]]
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[[Category: Yee, V.C.]]
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[[Category: Yee VC]]
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[[Category: acyltransferase]]
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[[Category: blood coagulation]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 22:14:33 2007''
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Current revision

RECOMBINANT HUMAN COAGULATION FACTOR XIII

PDB ID 1fie

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