1pi2: Difference between revisions

Line 1:

[[Image:1pi2.jpg|left|200px]]<br /><applet load="1pi2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1pi2.jpg|left|200px]]<br /><applet load="1pi2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1pi2, resolution 2.5Å" />

'''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PI2 OCA].

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==

Line 15:

[[Category: Chen, P.]]

[[Category: Rose, J.]]

[[Category: Wang, B.C.]]

[[Category: Wang, B C.]]

[[Category: serine proteinase inhibitor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 23~~:49:~~52 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:00 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1pi2.jpg|left|200px]]<br /><applet load="1pi2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pi2.jpg|left|200px]]<br /><applet load="1pi2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pi2, resolution 2.5&Aring;" />
 '''REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS'''<br />
 ==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.
+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==
-PI2 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PI2 OCA].
+PI2 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==
@@ Line 15: / Line 15: @@
 [[Category: Chen, P.]]
 [[Category: Rose, J.]]
-[[Category: Wang, B.C.]]
+[[Category: Wang, B C.]]
 [[Category: serine proteinase inhibitor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:49:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:00 2008''