ニュース

2016年07月15日 掲載 (Published 07/15/2016)


「Biophysics and Physicobiology」に 〈Special Issue: "Protein-Ligand Interactions"〉 Kazunori D. Yamada et al. “Structural characterization of single nucleotide variants at ligand binding sites and enzyme active sites of human proteins”を掲載

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Kazunori D. Yamada, Hafumi Nishi, Junichi Nakata, Kengo Kinoshita
“Structural characterization of single nucleotide variants at ligand binding sites and enzyme active sites of human proteins”

【Significance】
Human genetic variants at ligand binding sites and enzyme active sites

Functional sites on proteins play a key part in molecular interactions and reactions. Thus, mutations in functional sites can severely affect the overall phenotype. To understand the influence of genetic variants at a protein level, we investigated the relationship between single nucleotide variants and functional sites in terms of minor allele frequency and the structural position of variants. We found that variants were less abundant at ligand binding sites, and non-rare variants tended to be located slightly apart from enzyme active sites. Most of non-rare mutations were moderate changes of the physico-chemical properties, suggesting the existence of functional constraints.


Biophysics and Physicobiology, Vol.13, pp. 157-163

URL:https://www.jstage.jst.go.jp/article/biophysico/13/0/13_157/_article