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[[Image:1ex0.png|left|200px]]


{{STRUCTURE_1ex0|  PDB=1ex0  |  SCENE=  }}
==HUMAN FACTOR XIII, MUTANT W279F ZYMOGEN==
 
<StructureSection load='1ex0' size='340' side='right'caption='[[1ex0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
===HUMAN FACTOR XIII, MUTANT W279F ZYMOGEN===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1ex0]] 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=1EX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EX0 FirstGlance]. <br>
{{ABSTRACT_PUBMED_015576029}}
</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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ex0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ex0 OCA], [https://pdbe.org/1ex0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ex0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ex0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ex0 ProSAT]</span></td></tr>
[[1ex0]] is a 2 chain structure with 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=1EX0 OCA].  
</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/ex/1ex0_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=1ex0 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Factor XIII|Factor XIII]]
*[[Factor XIII|Factor XIII]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015576029</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-glutamine gamma-glutamyltransferase]]
[[Category: Large Structures]]
[[Category: Bishop, P D.]]
[[Category: Bishop PD]]
[[Category: Garzon, R J.]]
[[Category: Garzon RJ]]
[[Category: Pratt, K P.]]
[[Category: Le Trong I]]
[[Category: Stenkamp, R E.]]
[[Category: Pratt KP]]
[[Category: Teller, D C.]]
[[Category: Stenkamp RE]]
[[Category: Trong, I Le.]]
[[Category: Teller DC]]
[[Category: Blood coagulation]]
[[Category: Mutant]]
[[Category: Oxyanion]]
[[Category: Transferase]]
[[Category: Transglutaminase]]
[[Category: W279f]]

Latest revision as of 10:07, 7 February 2024

HUMAN FACTOR XIII, MUTANT W279F ZYMOGENHUMAN FACTOR XIII, MUTANT W279F ZYMOGEN

Structural highlights

1ex0 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 2Å
Ligands:, , ,
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

1ex0, resolution 2.00Å

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