1pi2: Difference between revisions

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{{STRUCTURE_1pi2|  PDB=1pi2  |  SCENE=  }}  
{{STRUCTURE_1pi2|  PDB=1pi2  |  SCENE=  }}  


'''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS'''
===REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS===




==Overview==
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The three-dimensional structure of the Bowman-Birk type proteinase inhibitor (PI-II) has been determined by x-ray crystallography and refined at 2.5-A resolution. This protein is a specific inhibitor of trypsin. Two reactive site loops, one at each end of the PI-II molecule, are structurally similar to each other and to reactive-site loops of pancreatic secretory trypsin inhibitor (Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E., and Huber, R. (1982) J. Mol. Biol. 162, 839-869) and bovine pancreatic trypsin inhibitor (Deisenhofer, J., and Steigemann, W. (1975) Acta Crystallogr. B31, 238-250). PI-II is the first reported Bowman-Birk type inhibitor structure to be refined at high resolution, providing further insight into inhibitor mechanisms.
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==About this Structure==
==About this Structure==
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[[Category: Wang, B C.]]
[[Category: Wang, B C.]]
[[Category: Serine proteinase inhibitor]]
[[Category: Serine proteinase inhibitor]]
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