Abstract
A protease inhibitor (CmPI-II) (UNIPROT: IPK2_CENMR) from the marine mollusc Cenchritis muricatus, has been isolated and characterized. It is the first member of a new group (group 3) of non-classical Kazal-type inhibitors. CmPI-II is a tight-binding inhibitor of serine proteases: trypsin, human neutrophil elastase (HNE), subtilisin A and pancreatic elastase. This specificity is exceptional in the members of Kazal-type inhibitor family. Several models of three-dimensional structure of CmPI-II have been constructed by homology with other inhibitors of the family but its structure has not yet been solved experimentally. Here we report the 1H, 15N and 13C chemical shift assignments of CmPI-II as basis for NMR structure determination and interaction studies. Secondary structure analyses deduced from the NMR chemical shift data have identified three β-strands β1: residues 14–19, β2: 23–35 and β3: 43–45 and one helix α1: 28–37 arranged in the sequential order β1–β2–α1–β3. These secondary structure elements suggest that CmPI-II adopts the typical scaffold of a Kazal-type inhibitor.
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The authors acknowledge founding from agencies FAPERJ, TWAS/CNPq and CAPES/MES-Cuba.
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Cabrera-Muñoz, A., Rojas, L., Alonso-del-Rivero Antigua, M. et al. 1H, 13C and 15N resonance assignments and secondary structure analysis of CmPI-II, a serine protease inhibitor isolated from marine snail Cenchritis muricatus . Biomol NMR Assign 10, 153–156 (2016). https://doi.org/10.1007/s12104-015-9656-5
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DOI: https://doi.org/10.1007/s12104-015-9656-5