4kty: Difference between revisions
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==Fibrin-stabilizing factor with a bound ligand== | ==Fibrin-stabilizing factor with a bound ligand== | ||
<StructureSection load='4kty' size='340' side='right' caption='[[4kty]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='4kty' size='340' side='right'caption='[[4kty]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4kty]] is a 4 chain structure with sequence from [ | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" | </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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == 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 == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 24: | Line 20: | ||
</div> | </div> | ||
<div class="pdbe-citations 4kty" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4kty" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Factor XIII|Factor XIII]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Heine | [[Category: Heine A]] | ||
[[Category: Klebe | [[Category: Klebe G]] | ||
[[Category: Stieler | [[Category: Stieler M]] | ||
Revision as of 09:13, 7 December 2022
Fibrin-stabilizing factor with a bound ligand
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