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• 作者：Aymara Cabrera-Muñoz ; Laritza Rojas…
• 关键词：Serine protease inhibitor ; Kazal ; type protease inhibitor ; NMR assignments ; Protein structure
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：10
• 期：1
• 页码：153-156
• 全文大小：577 KB
• 参考文献：Arastu-Kapur S, Ponder EL, Fonović UP, Yeoh S, Yuan F, Fonović M, Grainger M, Phillips CI, Powers JC, Bogyo M (2008) Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum. Nat Chem Biol 4:203–213CrossRef
  Cavanagh J, Fairbrother WJ, Palmer AG III, Rance M, Skelton NJ (2007) Protein NMR spectroscopy. Principles and practice, 2nd edn. Elsevier Academic Press, San Diego
  González Y, Tanaka YS, Hirata IY, Alonso del Rivero M, Oliva MLV, Araujo MS, Chavez MA (2007a) Purification and partial characterization of human neutrophil elastase inhibitors from the marine snail Cenchritis muricatus (Mollusca). Comp Biochem Physiol A: Mol Integr Physiol 146:506–513CrossRef
  González Y, Pons T, Gil J, Besada V, Alonso-del-Rivero M, Tanaka AS, Araujo MS, Chávez MA (2007b) Characterization and comparative 3D modeling of CmPI-II, a novel ‘non-classical’ Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca). Biol Chem 388:1183–1194CrossRef
  Kim K (2004) Role of proteases in host cell invasion by Toxoplasma gondii and other Apicomplexa. Acta Trop 91:69–81CrossRef
  Koussis K, Withers-Martinez C, Yeoh S, Child M, Hackett F, Knuepfer E, Juliano L, Woehlbier U, Bujard H, Blackman MJ (2009) A multifunctional serine protease primes the malaria parasite for red blood cell invasion. EMBO J 28:725–735CrossRef
  Rimphanitchayakit V, Tassanakajon A (2010) Structure and function of invertebrate Kazal type serine proteinase inhibitors. Dev Comp Immunol 34:377–386CrossRef
  Shen Y, Delaglio F, Cornilescu G, Bax A (2009) Talos+: a hybrid method for predicting protein backbone torsion angle from NMR chemical shifts. J Biomol NMR 44:213–223CrossRef
  
• 作者单位：Aymara Cabrera-Muñoz (1)
  Laritza Rojas (1)
  Maday Alonso-del-Rivero Antigua (1)
  José Ricardo Pires (2)
  
  1. Centro de Estudios de Proteínas, Facultad de Biología, Universidad de La Habana, Ciudad de La Habana-Cuba, 25 No. 455, Vedado, Havana, Cuba
  2. Instituto de bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Av. Carlos Chagas Filho, 373 - Bloco E, sala 10, 21941-902, Rio de Janeiro, RJ, Brazil
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

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.