1pi2
From Proteopedia
(New page: 200px<br /><applet load="1pi2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pi2, resolution 2.5Å" /> '''REACTIVE SITES OF AN ...) |
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| - | [[Image:1pi2.jpg|left|200px]]<br /><applet load="1pi2" size=" | + | [[Image:1pi2.jpg|left|200px]]<br /><applet load="1pi2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pi2, resolution 2.5Å" /> | caption="1pi2, resolution 2.5Å" /> | ||
'''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS'''<br /> | '''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the Bowman-Birk type proteinase | + | 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== | ==About this Structure== | ||
| - | 1PI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http:// | + | 1PI2 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Chen, P.]] | [[Category: Chen, P.]] | ||
[[Category: Rose, J.]] | [[Category: Rose, J.]] | ||
| - | [[Category: Wang, B | + | [[Category: Wang, B C.]] |
[[Category: serine proteinase inhibitor]] | [[Category: serine proteinase inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:00 2008'' |
Revision as of 12:29, 21 February 2008
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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
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