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Secondary structures, dynamics, and DNA binding of the homeodomain of human SIX1.
Li, Yan; Ng, Elizabeth YiHui; Loh, Ying Ru; Gea, Chong Yu; Huang, Qiwei; Li, Qingxin; Kang, CongBao.
Afiliação
  • Li Y; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore.
  • Ng EY; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore.
  • Loh YR; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore.
  • Gea CY; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore.
  • Huang Q; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore.
  • Li Q; Guangdong Provincial Engineering Laboratory of Biomass High Value Utilization, Institute of Biological and Medical Engineering, Guangdong Academy of Sciences, Guangzhou, China.
  • Kang C; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR), Singapore.
J Pept Sci ; 28(4): e3376, 2022 Apr.
Article em En | MEDLINE | ID: mdl-34713534
ABSTRACT
Human sine oculis homeobox homolog (SIX) 1 contains a homeodomain (HD), which is important for binding to DNA. In this study, we carried out structural studies on the HD of human SIX1 using nuclear magnetic resonance (NMR) spectroscopy. Its secondary structures and dynamics in solution were explored. HD is well-structured in solution, and our study shows that it contains three α-helices. Dynamics study indicates that the N- and C-terminal residues of HD are flexible in solution. HD of human SIX1 exhibits molecular interactions with a short double-strand DNA sequence evidenced by the 1 H-15 N-heteronuclear single quantum correlation (HSQC) and 19 F-NMR experiments. Our current study provides structural information for HD of human SIX1. Further studies indicate that this construct can be utilized to study SIX1 and DNA interactions.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: DNA / Proteínas de Homeodomínio Limite: Humans Idioma: En Revista: J Pept Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Singapura

Texto completo: 1 Base de dados: MEDLINE Assunto principal: DNA / Proteínas de Homeodomínio Limite: Humans Idioma: En Revista: J Pept Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Singapura