1btp: Difference between revisions

Line 1:

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

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

caption="1btp, resolution 2.2Å" />

'''UNIQUE BINDING OF A NOVEL SYNTHETIC INHIBITOR, N-[3-[4-[4-(AMIDINOPHENOXY)-CARBONYL]PHENYL]-2-METHYL-2-PROPENOYL]-N-ALLYLGLYCINE METHANESULFONATE TO BOVINE TRYPSIN, REVEALED BY THE CRYSTAL STRUCTURE OF THE COMPLEX'''<br />

==Overview==

Trypsin and, N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]-, N-allylglycine methanesulfonate (1), a newly designed and orally active, synthetic trypsin inhibitor, were cocrystallized. The space group of the, crystal is P2(1)2(1)2(1) with cell constants a = 63.74 A, b = 63.08 A, and, c = 69.38 A, which is nearly identical to that of the orthorhombic crystal, of guanidinobenzoyltrypsin. The structure was refined to a, crystallographic residual R = 0.176. The refined model of the 1-trypsin, complex provides the structural basis for the reaction mechanism of 1. On, the basis of the present X-ray results, it is proposed that the potent, inhibitory activity of 1 is mainly due to the formation of an acylated, trypsin through an "inverse substrate mechanism" and its low rate of, deacylation.

Trypsin and N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]- N-allylglycine methanesulfonate (1), a newly designed and orally active synthetic trypsin inhibitor, were cocrystallized. The space group of the crystal is P2(1)2(1)2(1) with cell constants a = 63.74 A, b = 63.08 A, and c = 69.38 A, which is nearly identical to that of the orthorhombic crystal of guanidinobenzoyltrypsin. The structure was refined to a crystallographic residual R = 0.176. The refined model of the 1-trypsin complex provides the structural basis for the reaction mechanism of 1. On the basis of the present X-ray results, it is proposed that the potent inhibitory activity of 1 is mainly due to the formation of an acylated trypsin through an "inverse substrate mechanism" and its low rate of deacylation.

==About this Structure==

1BTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1BTP OCA].

1BTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTP OCA].

==Reference==

Line 25:

[[Category: hydrolase (serine proteinase)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:54:~~51 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:58 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1btp.gif|left|200px]]<br /><applet load="1btp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1btp.gif|left|200px]]<br /><applet load="1btp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1btp, resolution 2.2&Aring;" />
 '''UNIQUE BINDING OF A NOVEL SYNTHETIC INHIBITOR, N-[3-[4-[4-(AMIDINOPHENOXY)-CARBONYL]PHENYL]-2-METHYL-2-PROPENOYL]-N-ALLYLGLYCINE METHANESULFONATE TO BOVINE TRYPSIN, REVEALED BY THE CRYSTAL STRUCTURE OF THE COMPLEX'''<br />
 ==Overview==
-Trypsin and, N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]-, N-allylglycine methanesulfonate (1), a newly designed and orally active, synthetic trypsin inhibitor, were cocrystallized. The space group of the, crystal is P2(1)2(1)2(1) with cell constants a = 63.74 A, b = 63.08 A, and, c = 69.38 A, which is nearly identical to that of the orthorhombic crystal, of guanidinobenzoyltrypsin. The structure was refined to a, crystallographic residual R = 0.176. The refined model of the 1-trypsin, complex provides the structural basis for the reaction mechanism of 1. On, the basis of the present X-ray results, it is proposed that the potent, inhibitory activity of 1 is mainly due to the formation of an acylated, trypsin through an "inverse substrate mechanism" and its low rate of, deacylation.
+Trypsin and N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]- N-allylglycine methanesulfonate (1), a newly designed and orally active synthetic trypsin inhibitor, were cocrystallized. The space group of the crystal is P2(1)2(1)2(1) with cell constants a = 63.74 A, b = 63.08 A, and c = 69.38 A, which is nearly identical to that of the orthorhombic crystal of guanidinobenzoyltrypsin. The structure was refined to a crystallographic residual R = 0.176. The refined model of the 1-trypsin complex provides the structural basis for the reaction mechanism of 1. On the basis of the present X-ray results, it is proposed that the potent inhibitory activity of 1 is mainly due to the formation of an acylated trypsin through an "inverse substrate mechanism" and its low rate of deacylation.
 ==About this Structure==
-BTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BTP OCA].
+BTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTP OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: hydrolase (serine proteinase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:54:51 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:58 2008''