6a8p

Transglutaminase 2 mutant G224V in complex with GTP

spinqualitylabelsall models 6a8p, resolution 2.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a8p is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.537Å Ligands: GTP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TGM2_HUMAN Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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