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Napoleão F. Valadares, Rodrigo de Oliveira-Silva, Italo A. Cavini, Ivo de Almeida Marques, Humberto D'Muniz Pereira, Andrea Soares-Costa, Flavio Henrique-Silva, Hans R. Kalbitzer, Claudia E. Munte and Richard C. Garratt X-ray crystallography and NMR studies of domain-swapped canecystatin-1 The FEBS Journal 280

Version of Record online: 11 JAN 2013 | DOI: 10.1111/febs.12095

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The three dimensional structure of canecystatin-1, a potent inhibitor of cysteine proteases from sugar cane, has been solved in two different crystal forms. In both cases it is seen to exist as a domain-swapped dimer, the first such observation is for a cystatin of plant origin. Size exclusion chromatography and multi-dimensional NMR spectroscopy show the dimer to be the dominant species in solution

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