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Backbone NMR assignments of the FAS1-3/FAS1-4 domains of transforming growth factor-beta-induced protein
- Authors
- Kang, Dong-Hoon; Yi, Jong-Jae; Sim, Dae-Won; Park, Jung-Wook; Lee, Sung-Hee; Kim, Eun-Hee; Jeon, Young-Ho; Son, Woo Sung; Won, Hyung-Sik; Kim, Ji-Hun
- Issue Date
- 2020
- Publisher
- KOREAN MAGNETIC RESONANCE SOC
- Keywords
- Blvrb; dialysis using micro-dialyzer; 1-dimensional HSQC experiment; N-15-labeled protein; protein refolding
- Citation
- JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY, v.24, no.1, pp.1 - 8
- Indexed
- KCI
- Journal Title
- JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY
- Volume
- 24
- Number
- 1
- Start Page
- 1
- End Page
- 8
- ISSN
- 1226-6531
- Abstract
- An extracellular matrix protein, transforming growth factor-beta-induced protein (TGFBIp/beta ig-h3), which is induced by transforming growth factor-beta 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.
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Related Researcher
- JEON, Young Ho
- College of Pharmacy (Department of Pharmaceutical Science)