In silico studies of the open form of human tissue transglutaminase.

ABSTRACT: Human tissue transglutaminase (tTG) is an intriguing multifunctional enzyme involved in various diseases, including celiac disease and neurological disorders. Although a number of tTG inhibitors have been developed, the molecular determinants governing ligand binding remain incomplete due to the lack of high-resolution structural data in the vicinity of its active site. In this study, we obtained the complete high-resolution model of tTG by in silico methods based on available PDB structures. We discovered significant differences in the active site architecture between our and known tTG models, revealing an additional loop which affects the ligand binding affinity. We assembled a library of new potential tTG inhibitors based on the obtained complete model of the enzyme. Our library substan

SUBMITTER: Ivashchenko SD 

PROVIDER: S-EPMC11236986 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature