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 journalArticlepeer-review

4 Scopus citations


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
Issue number2
StatePublished - Oct 2013
Externally publishedYes


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

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry


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