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Publication Abstract from PubMed

A cDNA encoding a cysteine protease inhibitor, cystatin was cloned from sesame (Sesamum indicum L.) seed. This clone was constructed into an expression vector and expressed in E. coli and purified to homogeneous. The recombinant sesame cystatin (SiCYS) showed effectively inhibitory activity toward C1 cysteine proteases. In order to unravel its inhibitory action from structural point of view, multidimensional heteronuclear NMR techniques were used to characterize the structure of SiCYS. The full (1)H, (15)N, and (13)C resonances of SiCYS were assigned. The secondary structure of SiCYS was identified by using the assigned chemical shifts of (1)H(alpha), (13)C(alpha), (13)C(beta), and (13)CO through the consensus chemical shift index (CSI). The results of CSI analysis of SiCYS suggest eight beta-strands (residues 33-46, 51-61, 63-75, 80-87, 150-155, 157-169, 172-183, and 192-195) and two alpha-helices (residues 16-30, and 120-135).

Resonance assignments and secondary structure of a phytocystatin from Sesamum indicum.,Hu YJ, Irene D, Lo CJ, Cai YL, Tzen TC, Lin TH, Chyan CL Biomol NMR Assign. 2015 Oct;9(2):309-11. doi: 10.1007/s12104-015-9598-y. Epub, 2015 Feb 12. PMID:25673506^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.