Interaction of troponin I and troponin C: use of the two-dimensional transferred nuclear Overhauser effect to determine the structure of a Gly-110 inhibitory troponin I peptide analog when bound to cardiac troponin C

A. Patricia Campbell, Jennifer E. Van Eyk, Robert S. Hodges, Brian D. Sykes

Research output: Contribution to journalArticle

Abstract

The structure of a peptide analog of the inhibitory region of cardiac troponin-1 (N-acetyl-G110-TnI(104-115)amide) when bound to cardiac troponin-C has been determined by 2-dimensional 1H-NMR techniques. The bound structure determined for this peptide is similar to that determined previously for the skeletal peptide (which has a proline at position 110) bound to skeletal troponin-C (Campbell and Sykes (1991) J. Mol. Biol. 222, 405-412). This structure shows a helical like peptide backbone "bent" around P109-G110 to bring the hydrophobic residues F1106, L111 and V114 closer together. The other "side" of this structure is surrounded by the basic residues extending outwards towards the protein or solution. While the bound structures of the cardiac and skeletal peptides are shown to be quite similar, the cardiac peptide appears more flexible near the central glycine residue.

Original languageEnglish (US)
Pages (from-to)35-54
Number of pages20
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1160
Issue number1
DOIs
StatePublished - Nov 10 1992

Keywords

  • (Heart)
  • Nuclear Overhauser effect
  • Troponin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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