Chemical shift assignments of the canecystatin-1 from Saccharum officinarum |
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Authors: | Ítalo Augusto Cavini Rodrigo de Oliveira-Silva Ivo de Almeida Marques Hans Robert Kalbitzer Claudia Elisabeth Munte |
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Affiliation: | 1. Physics Institute of S?o Carlos, University of S?o Paulo, Av. Trabalhador S?ocarlense 400, 13566-590, S?o Carlos, SP, Brazil 2. Physics Institute, Federal University of Goiás, 74001-970, Goiania, GO, Brazil 3. Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93047, Regensburg, Germany
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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. |
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