A functional role for correlated motion in the N-terminal RNA-binding domain of human U1A protein

Scott A. Showalter, Kathleen B. Hall

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

The N-terminal RNA-binding domain of the human U1A protein (RBD1) undergoes local conformational changes upon binding to its target RNA. Here, the wild-type RBD1 and two mutants are examined with molecular dynamics simulations that are analyzed using the reorientational eigen-mode dynamics (RED) formalism. The results reveal changes in the magnitude and extent of coupled intra-domain motions resulting from single amino acid substitutions. Interpretation of the novel RED results and corresponding NMR relaxation data suggests that the loss of collective motions in the mutants could account for their weak RNA-binding.

Original languageEnglish
Pages (from-to)533-542
Number of pages10
JournalJournal of Molecular Biology
Volume322
Issue number3
DOIs
StatePublished - Jan 1 2002

Keywords

  • Molecular dynamics simulations
  • NMR dynamics
  • RNA-binding domain
  • Reorientational eigenmode dynamics
  • U1A protein

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