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1pi2
From Proteopedia
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| - | [[Image:1pi2.jpg|left|200px]] | + | [[Image:1pi2.jpg|left|200px]] |
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| - | '''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS''' | + | {{Structure |
| + | |PDB= 1pi2 |SIZE=350|CAPTION= <scene name='initialview01'>1pi2</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PI2 is a [ | + | 1PI2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PI2 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1730730 1730730] |
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine proteinase inhibitor]] | [[Category: serine proteinase inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:24:35 2008'' |
Revision as of 11:24, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS
Overview
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.
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 Thu Mar 20 13:24:35 2008
