X-ray crystallography and NMR studies of domain-swapped canecystatin-1
Article first published online: 11 JAN 2013
© 2012 The Authors Journal compilation © 2012 FEBS
Volume 280, Issue 4, pages 1028–1038, February 2013
How to Cite
Valadares, N. F., de Oliveira-Silva, R., Cavini, I. A., de Almeida Marques, I., D'Muniz Pereira, H., Soares-Costa, A., Henrique-Silva, F., Kalbitzer, H. R., Munte, C. E. and Garratt, R. C. (2013), X-ray crystallography and NMR studies of domain-swapped canecystatin-1. FEBS Journal, 280: 1028–1038. doi: 10.1111/febs.12095
- Issue published online: 15 FEB 2013
- Article first published online: 11 JAN 2013
- Accepted manuscript online: 14 DEC 2012 07:53AM EST
- Manuscript Accepted: 3 DEC 2012
- Manuscript Revised: 29 NOV 2012
- Manuscript Received: 15 SEP 2012
- State of São Paulo Research Foundation. Grant Number: 08/58316-5 and 10/09100-0
Fig. S1. SDS/PAGE of the eluted peaks obtained in the SEC experiment shown in Fig. 1.
Fig. S2. DLS data for the His-tag-free protein.
Fig. S3. Omit map of Val60, Val61, Ala62, and Gly63, which form the open interface in domain-swapped dimers and the first inhibitory loop in monomers.
Fig. S4. Sequence alignment of the phytocystatins canecystatin-1, tarocystatin, oryzacystatin-1, and pineapple cystatin, together with human cystatin C.
Fig. S5. Comparison between canecystatin-1, stefin B, and human cystatin C.
Fig. S6. Particularities within the canecystatin-1 β-sheet.
Table S1. Angle between the helices in domain-swapped cystatin dimers.
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