1H, 13C and 15N resonance assignments and secondary structure analysis of CmPI-II, a serine protease inhibitor isolated from marine snail Cenchritis muricatus
| Autor: | Maday Alonso-del-Rivero Antigua, José R. Pires, Laritza Rojas, Aymara Cabrera-Muñoz |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Serine protease Proteases Serine Proteinase Inhibitors Kunitz STI protease inhibitor Stereochemistry Snails Biology Cenchritis muricatus Trypsin biology.organism_classification Biochemistry Protein Structure Secondary 03 medical and health sciences 030104 developmental biology Structural Biology medicine biology.protein Animals Nuclear Magnetic Resonance Biomolecular Pancreatic elastase Protein secondary structure medicine.drug |
| Zdroj: | Biomolecular NMR Assignments. 10:153-156 |
| ISSN: | 1874-270X 1874-2718 |
| DOI: | 10.1007/s12104-015-9656-5 |
| Popis: | 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 (1)H, (15)N and (13)C 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. |
| Databáze: | OpenAIRE |
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