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http://dx.doi.org/10.6564/JKMRS.2020.24.1.001

Backbone NMR assignments of the FAS1-3/FAS1-4 domains of transforming growth factor-beta-induced protein  

Kang, Dong-Hoon (College of Pharmacy, Chungbuk National University)
Yi, Jong-Jae (Department of Pharmacy, College of Pharmacy and Institute of Pharmaceutical Sciences, CHA University)
Sim, Dae-Won (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University)
Park, Jung-Wook (College of Pharmacy, Chungbuk National University)
Lee, Sung-Hee (College of Pharmacy, Chungbuk National University)
Kim, Eun-Hee (Research Center for Bioconvergence Analysis, Korea Basic Science Institute)
Jeon, Young-Ho (Korea University College of Pharmacy Sejong-ro)
Son, Woo Sung (Department of Pharmacy, College of Pharmacy and Institute of Pharmaceutical Sciences, CHA University)
Won, Hyung-Sik (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University)
Kim, Ji-Hun (College of Pharmacy, Chungbuk National University)
Publication Information
Journal of the Korean Magnetic Resonance Society / v.24, no.1, 2020 , pp. 1-8 More about this Journal
Abstract
An extracellular matrix protein, transforming growth factor-beta-induced protein (TGFBIp/βig-h3), which is induced by transforming growth factor-β in the human cornea, skin, and matrix of many connective tissues, is associated with the adhesion, migration, proliferation, and differentiation of various cells. TGFBIp contains four homologous repeat domains, known as FAS1 domains, where certain mutations have been considered to cause corneal dystrophies. In this study, backbone NMR assignments of FAS1-3/FAS1-4 tandem domain were obtained and compared with those previously known for the isolated FAS1-4 domain. The results corroborate in solution the inter-domain interaction between FAS1-3 and FAS1-4 in TGFBIp.
Keywords
Blvrb; dialysis using micro-dialyzer; 1-dimensional HSQC experiment; $^{15}N$-labeled protein; protein refolding;
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