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1pi2

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{{STRUCTURE_1pi2| PDB=1pi2 | SCENE= }}
{{STRUCTURE_1pi2| PDB=1pi2 | SCENE= }}
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'''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS'''
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===REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS===
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==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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{{ABSTRACT_PUBMED_1730730}}
==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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:03:01 2008''

Revision as of 14:03, 28 July 2008

Image:1pi2.png

Template:STRUCTURE 1pi2

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

Template:ABSTRACT PUBMED 1730730

About this Structure

1PI2 is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors., Chen P, Rose J, Love R, Wei CH, Wang BC, J Biol Chem. 1992 Jan 25;267(3):1990-4. PMID:1730730

Page seeded by OCA on Mon Jul 28 17:03:01 2008

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