4pyg

From Proteopedia

Transglutaminase2 complexed with GTP

Structural highlights

4pyg 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 2.8Å
Ligands:
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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jang TH, Lee DS, Choi K, Jeong EM, Kim IG, Kim YW, Chun JN, Jeon JH, Park HH. Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site. PLoS One. 2014 Sep 5;9(9):e107005. doi: 10.1371/journal.pone.0107005. eCollection, 2014. PMID:25192068 doi:http://dx.doi.org/10.1371/journal.pone.0107005