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

Michelle A. Markus, Andrew P. Hinck, Shengrong Huang, David E. Draper, Dennis A. Torchia

Research output: Contribution to journalArticle

77 Citations (Scopus)

Abstract

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 α1 and strand β1 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 α3 are involved in RNA binding.

Original languageEnglish (US)
Pages (from-to)70-77
Number of pages8
JournalNature Structural Biology
Volume4
Issue number1
DOIs
StatePublished - Jan 1997
Externally publishedYes

Fingerprint

RNA
Proteins
Chemical shift
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
ribosomal protein L11
C 76

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. / Markus, Michelle A.; Hinck, Andrew P.; Huang, Shengrong; Draper, David E.; Torchia, Dennis A.

In: Nature Structural Biology, Vol. 4, No. 1, 01.1997, p. 70-77.

Research output: Contribution to journalArticle

Markus, Michelle A. ; Hinck, Andrew P. ; Huang, Shengrong ; Draper, David E. ; Torchia, Dennis A. / High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. In: Nature Structural Biology. 1997 ; Vol. 4, No. 1. pp. 70-77.
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