Secondary structures, dynamics, and DNA binding of the homeodomain of human SIX1

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...

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Bibliographic Details
Published in:Journal of peptide science 2022-04, Vol.28 (4), p.e3376-n/a
Main Authors: Li, Yan, Ng, Elizabeth YiHui, Loh, Ying Ru, Gea, Chong Yu, Huang, Qiwei, Li, Qingxin, Kang, CongBao
Format: Article
Language:English
Subjects:
Binding
Deoxyribonucleic acid
DNA
DNA binding
Dynamic structural analysis
Helices
Homeobox
Homeodomain Proteins - chemistry
Homeodomain Proteins - genetics
Homeodomain Proteins - metabolism
Homology
Humans
Molecular interactions
NMR
NMR spectroscopy
Nuclear magnetic resonance
Nucleotide sequence
Peptides
protein dynamics
Protein Structure, Secondary
SIX gene family
SIX1
Spectroscopy
transcription factor
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Summary: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 1H‐15N‐heteronuclear single quantum correlation (HSQC) and 19F‐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. SIX1 HD is well‐structured and contains three α‐helices in solution. Dynamics study indicates that the N‐ and C‐terminal residues of HD are flexible in solution. SIX1 HD exhibits molecular interactions with a short double‐strand DNA sequence. Our current study provides structural information for SIX1 HD.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.3376