4pyg
From Proteopedia
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| - | ''' | + | ==Transglutaminase2 complexed with GTP== |
| + | <StructureSection load='4pyg' size='340' side='right' caption='[[4pyg]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4pyg]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PYG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PYG FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pyg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pyg RCSB], [http://www.ebi.ac.uk/pdbsum/4pyg PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TGM2_HUMAN TGM2_HUMAN]] Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transglutaminase2 (TG2) is a multi-functional protein involved in various cellular processes, including apoptosis, differentiation, wound healing, and angiogenesis. The malfunction of TG2 causes many human disease including inflammatory disease, celiac disease, neurodegenerative diseases, tissue fibrosis, and cancers. Protein cross-linking activity, which is representative of TG2, is activated by calcium ions and suppressed by GTP. Here, we elucidated the structure of TG2 in complex with its endogenous inhibitor, GTP. Our structure showed why GTP is the optimal nucleotide for interacting with and inhibiting TG2. In addition, sequence comparison provided information describing the evolutionary scenario of GTP usage for controlling the activity of TG2. | ||
| - | + | Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site.,Jang TH, Lee DS, Choi K, Jeong EM, Kim IG, Kim YW, Chun JN, Jeon JH, Park HH PLoS One. 2014 Sep 5;9(9):e107005. doi: 10.1371/journal.pone.0107005. eCollection, 2014. PMID:25192068<ref>PMID:25192068</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Park, H | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Protein-glutamine gamma-glutamyltransferase]] | ||
| + | [[Category: Jang, T H]] | ||
| + | [[Category: Park, H H]] | ||
| + | [[Category: Crosslinking]] | ||
| + | [[Category: Gtp binding]] | ||
| + | [[Category: No modification]] | ||
| + | [[Category: Protein-gtp complex]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Transglutaminase fold]] | ||
Revision as of 11:48, 12 February 2015
Transglutaminase2 complexed with GTP
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