1ggt

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(New page: 200px<br /> <applet load="1ggt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggt, resolution 2.65&Aring;" /> '''THREE-DIMENSIONAL S...)
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[[Image:1ggt.gif|left|200px]]<br />
 
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<applet load="1ggt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ggt, resolution 2.65&Aring;" />
 
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'''THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII'''<br />
 
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==Overview==
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==THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII==
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Mechanical stability in many biological materials is provided by the, crosslinking of large structural proteins with, gamma-glutamyl-epsilon-lysyl amide bonds. The three-dimensional structure, of human recombinant factor XIII (EC 2.3.2.13 zymogen;, protein-glutamine:amine gamma-glutamyltransferase a chain), a, transglutaminase zymogen, has been solved at 2.8-A resolution by x-ray, crystallography. This structure shows that each chain of the homodimeric, protein is folded into four sequential domains. A catalytic triad, reminiscent of that observed in cysteine proteases has been identified in, the core domain. The amino-terminal activation peptide of each subunit, crosses the dimer interface and partially occludes the opening of the, catalytic cavity in the second subunit, preventing substrate binding to, the zymogen. A proposal for the mechanism of activation by thrombin and, calcium is made that details the structural events leading to active, factor XIIIa'.
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<StructureSection load='1ggt' size='340' side='right'caption='[[1ggt]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ggt]] 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=1GGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GGT 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]] 2.65&#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=1ggt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggt OCA], [https://pdbe.org/1ggt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ggt RCSB], [https://www.ebi.ac.uk/pdbsum/1ggt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ggt 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/gg/1ggt_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=1ggt ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Factor XIIIA deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134570 134570]]
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*[[Factor XIII|Factor XIII]]
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== References ==
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==About this Structure==
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<references/>
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1GGT 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GGT OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII., Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC, Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7296-300. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7913750 7913750]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein-glutamine gamma-glutamyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bishop PD]]
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[[Category: Bishop, P.D.]]
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[[Category: Pedersen LC]]
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[[Category: Pedersen, L.C.]]
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[[Category: Stenkamp RE]]
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[[Category: Stenkamp, R.E.]]
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[[Category: Teller DC]]
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[[Category: Teller, D.C.]]
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[[Category: Trong IL]]
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[[Category: Trong, I.L.]]
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[[Category: Yee VC]]
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[[Category: Yee, V.C.]]
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[[Category: blood coagulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:05:01 2007''
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Current revision

THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE: HUMAN BLOOD COAGULATION FACTOR XIII

PDB ID 1ggt

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