View source for 4kty


==Fibrin-stabilizing factor with a bound ligand==
<StructureSection load='4kty' size='340' side='right'caption='[[4kty]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kty]] is a 4 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=4KTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KTY 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]] 1.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1TX:(2S)-2-AMINO-7-METHOXY-7-OXOHEPTANOIC+ACID'>1TX</scene>, <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DAS:D-ASPARTIC+ACID'>DAS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4kty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kty OCA], [https://pdbe.org/4kty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kty RCSB], [https://www.ebi.ac.uk/pdbsum/4kty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kty 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
On active duty: The available drugs for cardiovascular diseases can promote blood clotting but can also lead to life-threatening bleeding episodes. A promising target for the development of safer alternatives is the transglutaminase Factor XIII (FXIII), the active structure of which is presented. The binding and coordination of three calcium ions induce major domain movements in the enzyme upon activation.

Structure of Active Coagulation Factor XIII Triggered by Calcium Binding: Basis for the Design of Next-Generation Anticoagulants.,Stieler M, Weber J, Hils M, Kolb P, Heine A, Buchold C, Pasternack R, Klebe G Angew Chem Int Ed Engl. 2013 Sep 20. doi: 10.1002/anie.201305133. PMID:24115223<ref>PMID:24115223</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kty" style="background-color:#fffaf0;"></div>

==See Also==
*[[Factor XIII|Factor XIII]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Heine A]]
[[Category: Klebe G]]
[[Category: Stieler M]]