High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA

Nat Struct Biol. 1997 Jan;4(1):70-7. doi: 10.1038/nsb0197-70.


The structure of the C-terminal RNA recognition domain of ribosomal protein L11 has been solved by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. Although the structure can be considered high resolution in the core, 15 residues between helix alpha 1 and strand beta 1 form an extended, unstructured loop. 15N transverse relaxation measurements suggest that the loop is moving on a picosecond-to-nanosecond time scale in the free protein but not in the protein bound to RNA. Chemical shifts differences between the free protein and the bound protein suggest that the loop as well as the C-terminal end of helix alpha 3 are involved in RNA binding.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Protein Conformation
  • RNA / metabolism*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / metabolism
  • Solutions


  • RNA-Binding Proteins
  • Ribosomal Proteins
  • Solutions
  • ribosomal protein L11
  • RNA