Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca2+-calmodulin

Dmitry S Kanibolotsky, Oleksandra V Novosyl'na, Catherine M Abbott, Boris S Negrutskii, Anna V El'skaya

Research output: Contribution to journalArticlepeer-review

Abstract

Eukaryotic translation elongation factor eEF1A directs the correct aminoacyl-tRNA to ribosomal A-site. In addition, eEF1A is involved in carcinogenesis and apoptosis and can interact with large number of non-translational ligands. There are two isoforms of eEF1A, which are 98% similar. Despite the strong similarity, the isoforms differ in some properties. Importantly, the appearance of eEF1A2 in tissues in which the variant is not normally expressed can be coupled to cancer development.We reasoned that the background for the functional difference of eEF1A1 and eEF1A2 might lie in changes of dynamics of the isoforms.
Original languageEnglish
Pages (from-to)4
JournalBMC Structural Biology
Volume8
DOIs
Publication statusPublished - 2008

Keywords

  • Amino Acid Sequence
  • Binding Sites
  • Calcium
  • Calmodulin
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Elongation Factor 1
  • Protein Conformation
  • Protein Isoforms
  • Protein Structure, Tertiary
  • Sequence Alignment

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