Artículos de revistas
Chemical shift assignments of the canecystatin-1 from Saccharum officinarum
Fecha
2013-10Registro en:
Biomolecular NMR Assignments, Dordrecht : Springer, v. 7, n. 2, p. 163-165, Oct. 2013
1874-2718
10.1007/s12104-012-9401-2
Autor
Cavini, Ítalo Augusto
Silva, Rodrigo de Oliveira
Marques, Ivo de Almeida
Kalbitzer, Hans Robert
Munte, Claudia Elisabeth
Institución
Resumen
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.