6A8P
Transglutaminase 2 mutant G224V in complex with GTP
Summary for 6A8P
| Entry DOI | 10.2210/pdb6a8p/pdb |
| Descriptor | Protein-glutamine gamma-glutamyltransferase 2, GUANOSINE-5'-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | transglutaminase, complex, mutant, gtp, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 3 |
| Total formula weight | 237021.10 |
| Authors | Park, H.H.,Ha, H.J.,Kwon, S. (deposition date: 2018-07-09, release date: 2018-09-26, Last modification date: 2023-11-22) |
| Primary citation | Ha, H.J.,Kwon, S.,Jeong, E.M.,Kim, C.M.,Lee, K.B.,Kim, I.G.,Park, H.H. Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity. PLoS ONE, 13:e0204707-e0204707, 2018 Cited by PubMed Abstract: 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). PubMed: 30321187DOI: 10.1371/journal.pone.0204707 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.537 Å) |
Structure validation
Download full validation report
