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The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor (1975)

Huber, R. ; Bode, W. ; Kukla, D. ; [et al.]

Springer

European biophysics journal 1 (1975), S. 189-201

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ISSN: 1432-1017

Keywords: Trypsin ; Inhibitor ; Protein-Structure ; X-Ray Analysis ; Enzyme Substrate Interaction

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Physics

Notes: 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00535756

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