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Biophysics of structure and mechanism

, Volume 1, Issue 3, pp 189–201 | Cite as

The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor

III. Structure of the anhydro-trypsin-inhibitor complex
  • R. Huber
  • W. Bode
  • D. Kukla
  • U. Kohl
  • C. A. Ryan
Article

Abstract

The structure of the complex between anhydro-trypsin and pancreatic trypsin inhibitor has been determined by difference Fourier techniques using phases obtained from the native complex (Huber et al., 1974). It was refined independently by constrained crystallographic refinement at 1.9 å resolution. The anhydro-complex has Ser 195 converted to dehydro-alanine. There were no other significant structural changes. In particular, the high degree of pyramidalization of the C atom of Lys 15 (I) of the inhibitor component observed in the native complex is maintained in the anhydro-species.

Key words

Trypsin Inhibitor Protein-Structure X-Ray Analysis Enzyme Substrate Interaction 

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Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • R. Huber
    • 1
    • 2
  • W. Bode
    • 1
    • 2
  • D. Kukla
    • 1
    • 2
  • U. Kohl
    • 1
    • 2
  • C. A. Ryan
    • 3
  1. 1.Max-Planck-Institut für BiochemieGermany
  2. 2.Physikalisch-chemisches Institut der Technischen UniversitÄtMünchenGermany
  3. 3.Department of Agricultural ChemistryWashington State UniversityPullmanUSA

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