1fie: Difference between revisions

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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 molecule. This work shows that the activation peptide, upon thrombin cleavage, has the same conformation and occupies the same, position with respect to the rest of the molecule as it does in the, zymogen structure.
<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 Mon Nov  5 16:12:19 2007''

Latest revision as of 10:14, 7 February 2024

RECOMBINANT HUMAN COAGULATION FACTOR XIIIRECOMBINANT HUMAN COAGULATION FACTOR XIII

Structural highlights

1fie is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

F13A_HUMAN Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [MIM:613225. FA13AD is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.[1]

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Board P, Coggan M, Miloszewski K. Identification of a point mutation in factor XIII A subunit deficiency. Blood. 1992 Aug 15;80(4):937-41. PMID:1353995

1fie, resolution 2.50Å

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