Computational study of the impact of nucleotide variations on highly conserved proteins: In the case of actin

Ha T.T. Duong, Hirofumi Suzuki, Saki Katagiri, Mayu Shibata, Misae Arai, Kei Yura*

*この研究の対応する著者

研究成果: Comment/debate査読

抄録

Sequencing of individual human genomes enables studying relationship among nucleotide variations, amino acid substitutions, effect on protein structures and diseases. Many studies have found general tendencies, for instance, that pathogenic variations tend to be found in the buried regions of the protein structures, that benign variations tend to be found on the surface of the proteins, and that variations on evolutionary conserved residues tend to be pathogenic. These tendencies were deduced from globular proteins with standard evolutionary changes in amino acid sequences. In this study, we investigated the variation distribution on actin, one of the highly conserved proteins. Many nucleotide variations and three-dimensional structures of actin have been registered in databases. By combining those data, we found that variations buried inside the protein were rather benign and variations on the surface of the protein were pathogenic. This idiosyncratic distribution of the variation impact is likely ascribed to the extensive use of the surface of the protein for protein-protein interactions in actin.

本文言語English
論文番号e190025
ジャーナルBiophysics and physicobiology
19
DOI
出版ステータスPublished - 2022

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 生理学
  • 生化学、遺伝学、分子生物学(その他)

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