Chemical shift assignments of the canecystatin-1 from Saccharum officinarum

Ítalo Augusto Cavini, Rodrigo De Oliveira-Silva, Ivo De Almeida Marques, Hans Robert Kalbitzer, Claudia Elisabeth Munte

Research output: Contribution to journalArticle

Abstract

Cystatins are cysteine proteases inhibitors that are widely distributed among insects, mammalians and plants. Here we report the complete resonance assignment of canecystatin-1 from Saccharum officinarum obtained by heteronuclear multidimensional high-resolution nuclear magnetic resonance spectroscopy. The consensus chemical shift index was calculated and showed the presence of one α-helix (residues 27-43) and three β-strands (residues 48-74, 78-89 and 94-104), a secondary structure pattern that suggests a domain-swapped structure as presented by stefin B and human cystatin C, opposed to the monomeric structure yet found in other phytocystatins like oryza and pineapple cystatin.

Original languageEnglish (US)
Pages (from-to)163-165
Number of pages3
JournalBiomolecular NMR Assignments
Volume7
Issue number2
DOIs
StatePublished - Oct 2013
Externally publishedYes

Keywords

  • Canecystatin-1
  • Cysteine protease inhibitor
  • Phytocystatin
  • Saccharum officinarum cystatin

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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  • Cite this

    Cavini, Í. A., De Oliveira-Silva, R., De Almeida Marques, I., Kalbitzer, H. R., & Munte, C. E. (2013). Chemical shift assignments of the canecystatin-1 from Saccharum officinarum. Biomolecular NMR Assignments, 7(2), 163-165. https://doi.org/10.1007/s12104-012-9401-2