{"title":"Eliducating the Distinctions between Open-State Monomers and Dimers of Human Tissue Transglutaminase","authors":"S. D. Ivashchenko, A. V. Vlasov","doi":"10.1134/s1547477124701450","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Transglutaminase 2 (TG2) is a pivotal enzyme involved in various biological processes such as wound healing, apoptosis, and cell differentiation. Depending on the environmental conditions, TG2 can adopt two distinct conformations: the open and closed states. Notably, the open conformation of TG2 has been associated with the pathogenesis of several diseases, including celiac disease and certain cancers. Recent investigations have demonstrated that within human cells, open-state TG2 can exist both as monomers and as dimers. The monomeric form primarily exhibits transamidation activity, whereas the dimeric form is postulated to exert cytotoxic effects. While several structures of the monomeric open-state TG2 are available in the Protein Data Bank, structures representing the dimeric form remain elusive. The objective of this study is to elucidate the structural distinctions between TG2 monomers and dimers using small-angle X-ray scattering (SAXS).</p>","PeriodicalId":730,"journal":{"name":"Physics of Particles and Nuclei Letters","volume":"16 1","pages":""},"PeriodicalIF":0.4000,"publicationDate":"2024-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Physics of Particles and Nuclei Letters","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1134/s1547477124701450","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"PHYSICS, PARTICLES & FIELDS","Score":null,"Total":0}
引用次数: 0
Abstract
Transglutaminase 2 (TG2) is a pivotal enzyme involved in various biological processes such as wound healing, apoptosis, and cell differentiation. Depending on the environmental conditions, TG2 can adopt two distinct conformations: the open and closed states. Notably, the open conformation of TG2 has been associated with the pathogenesis of several diseases, including celiac disease and certain cancers. Recent investigations have demonstrated that within human cells, open-state TG2 can exist both as monomers and as dimers. The monomeric form primarily exhibits transamidation activity, whereas the dimeric form is postulated to exert cytotoxic effects. While several structures of the monomeric open-state TG2 are available in the Protein Data Bank, structures representing the dimeric form remain elusive. The objective of this study is to elucidate the structural distinctions between TG2 monomers and dimers using small-angle X-ray scattering (SAXS).
期刊介绍：
The journal Physics of Particles and Nuclei Letters, brief name Particles and Nuclei Letters, publishes the articles with results of the original theoretical, experimental, scientific-technical, methodological and applied research. Subject matter of articles covers: theoretical physics, elementary particle physics, relativistic nuclear physics, nuclear physics and related problems in other branches of physics, neutron physics, condensed matter physics, physics and engineering at low temperatures, physics and engineering of accelerators, physical experimental instruments and methods, physical computation experiments, applied research in these branches of physics and radiology, ecology and nuclear medicine.
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