Inhibitor Binding Induces Structural Changes in Porcine Pepsin

  • Cele Abad-Zapatero
  • T. J. Rydel
  • D. J. Neidhart
  • J. Luly
  • J. W. Erickson
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 306)


Crystal structures of several fungal aspartic proteinases have been refined at high resolution: penicillopepsin1, Endothia parasitica pepsin2 and Rhizopus chinensis protease.3 The structure of a recombinant form of human renin has been solved4 at 2.5 Å and the refined structures of two other mammalian aspartic proteinases have been reported recently: chymosin at 2.3 Å resolution5, and the monoclinic form of porcine pepsin at 2.3 and 1.8 Å resolution6,7, as well as the original hexagonal crystal form8.


Aspartic Proteinase Iodine Atom Fungal Enzyme Monoclinic Form Human Renin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Cele Abad-Zapatero
    • 1
  • T. J. Rydel
    • 1
  • D. J. Neidhart
    • 3
  • J. Luly
    • 2
  • J. W. Erickson
    • 1
  1. 1.Laboratory of Protein Crystallography, D-47EUSA
  2. 2.Cardiovascular Chemistry, D-47LAbbott LaboratoriesAbbott ParkUSA
  3. 3.Department of ChemistryMichigan State UniversityEast LansingUSA

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