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

doi:10.1007/s12104-012-9401-2

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 journal › Article › peer-review

4 Scopus citations

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 language	English (US)
Pages (from-to)	163-165
Number of pages	3
Journal	Biomolecular NMR Assignments
Volume	7
Issue number	2
DOIs	https://doi.org/10.1007/s12104-012-9401-2
State	Published - Oct 2013
Externally published	Yes

Keywords

Canecystatin-1
Cysteine protease inhibitor
Phytocystatin
Saccharum officinarum cystatin

ASJC Scopus subject areas

Structural Biology
Biochemistry

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10.1007/s12104-012-9401-2

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title = "Chemical shift assignments of the canecystatin-1 from Saccharum officinarum",

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.",

keywords = "Canecystatin-1, Cysteine protease inhibitor, Phytocystatin, Saccharum officinarum cystatin",

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doi = "10.1007/s12104-012-9401-2",

language = "English (US)",

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journal = "Biomolecular NMR Assignments",

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TY - JOUR

T1 - Chemical shift assignments of the canecystatin-1 from Saccharum officinarum

AU - Cavini, Ítalo Augusto

AU - De Oliveira-Silva, Rodrigo

AU - De Almeida Marques, Ivo

AU - Kalbitzer, Hans Robert

AU - Munte, Claudia Elisabeth

PY - 2013/10

Y1 - 2013/10

N2 - 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.

AB - 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.

KW - Canecystatin-1

KW - Cysteine protease inhibitor

KW - Phytocystatin

KW - Saccharum officinarum cystatin

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DO - 10.1007/s12104-012-9401-2

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Chemical shift assignments of the canecystatin-1 from Saccharum officinarum

Abstract

Keywords

ASJC Scopus subject areas

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