6a8p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:21, 22 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Transglutaminase 2 mutant G224V in complex with GTP==
==Transglutaminase 2 mutant G224V in complex with GTP==
-
<StructureSection load='6a8p' size='340' side='right' caption='[[6a8p]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
+
<StructureSection load='6a8p' size='340' side='right'caption='[[6a8p]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6a8p]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A8P FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6a8p]] is a 3 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=6A8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A8P 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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.537&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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=6a8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8p OCA], [http://pdbe.org/6a8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a8p RCSB], [http://www.ebi.ac.uk/pdbsum/6a8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8p ProSAT]</span></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=6a8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8p OCA], [https://pdbe.org/6a8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a8p RCSB], [https://www.ebi.ac.uk/pdbsum/6a8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8p ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/TGM2_HUMAN TGM2_HUMAN]] Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
+
[https://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 ==
 +
Multi-functional transglutaminase 2 (TG2), which possesses protein cross-linking and GTP hydrolysis activities, is involved in various cellular processes, including apoptosis, angiogenesis, wound healing, and neuronal regeneration, and is associated with many human diseases, including inflammatory disease, celiac disease, neurodegenerative disease, diabetes, tissue fibrosis, and cancers. Although most biochemical and cellular studies have been conducted with the TG2 (G224) form, the TG2 (G224V) form has recently emerged as a putative natural variant of TG2. In this study, we characterized the putative natural form of TG2, TG2 (G224V), and through a new crystal structure of TG2 (G224V), we revealed how TG2 (G224V) gained stability and higher Ca2+-dependent activity than an artificial variant of TG2 (G224).
 +
 
 +
Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity.,Ha HJ, Kwon S, Jeong EM, Kim CM, Lee KB, Kim IG, Park HH PLoS One. 2018 Oct 15;13(10):e0204707. doi: 10.1371/journal.pone.0204707., eCollection 2018. PMID:30321187<ref>PMID:30321187</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6a8p" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Protein-glutamine gamma-glutamyltransferase]]
+
[[Category: Homo sapiens]]
-
[[Category: Ha, H J]]
+
[[Category: Large Structures]]
-
[[Category: Kwon, S]]
+
[[Category: Ha HJ]]
-
[[Category: Park, H H]]
+
[[Category: Kwon S]]
-
[[Category: Complex]]
+
[[Category: Park HH]]
-
[[Category: Gtp]]
+
-
[[Category: Mutant]]
+
-
[[Category: Transferase]]
+
-
[[Category: Transglutaminase]]
+

Current revision

Transglutaminase 2 mutant G224V in complex with GTP

PDB ID 6a8p

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6a8p"
Personal tools