1tx8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1tx8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tx8, resolution 1.7&Aring;" /> '''Bovine Trypsin comple...)
Line 1: Line 1:
-
[[Image:1tx8.gif|left|200px]]<br /><applet load="1tx8" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1tx8.gif|left|200px]]<br /><applet load="1tx8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tx8, resolution 1.7&Aring;" />
caption="1tx8, resolution 1.7&Aring;" />
'''Bovine Trypsin complexed with AMSO'''<br />
'''Bovine Trypsin complexed with AMSO'''<br />
==Overview==
==Overview==
-
We have designed, synthesized, and evaluated the factor Xa inhibitory, activities of p-amidinophenyl-sulfones, amines, and alcohols intended to, take advantage of the polarity and hydrogen-bonding potential of the, oxyanion hole region of the S1 specificity pocket. We demonstrate that, placement of an anionic group within the oxyanion hole region of the, catalytic site substantially enhances activity, with small flexible groups, favored over bulkier ones. Ab initio pKa calculations suggest that the, hydroxyl substituent frequently used for benzamidine moieties may be, ionized to form an anionic group, consistent with the general trend. One, nonamidine based substituent also shows promising activity.
+
We have designed, synthesized, and evaluated the factor Xa inhibitory activities of p-amidinophenyl-sulfones, amines, and alcohols intended to take advantage of the polarity and hydrogen-bonding potential of the oxyanion hole region of the S1 specificity pocket. We demonstrate that placement of an anionic group within the oxyanion hole region of the catalytic site substantially enhances activity, with small flexible groups favored over bulkier ones. Ab initio pKa calculations suggest that the hydroxyl substituent frequently used for benzamidine moieties may be ionized to form an anionic group, consistent with the general trend. One nonamidine based substituent also shows promising activity.
==About this Structure==
==About this Structure==
-
1TX8 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 and AM4 as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1TX8 OCA].
+
1TX8 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> and <scene name='pdbligand=AM4:'>AM4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1TX8 OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trypsin]]
[[Category: Trypsin]]
-
[[Category: Mesecar, A.D.]]
+
[[Category: Mesecar, A D.]]
[[Category: AM4]]
[[Category: AM4]]
[[Category: CA]]
[[Category: CA]]
[[Category: trypsin]]
[[Category: trypsin]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:39:48 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:18 2008''

Revision as of 13:18, 21 February 2008

Image:1tx8.gif

1tx8, resolution 1.7Å

Drag the structure with the mouse to rotate

Bovine Trypsin complexed with AMSO

Overview

We have designed, synthesized, and evaluated the factor Xa inhibitory activities of p-amidinophenyl-sulfones, amines, and alcohols intended to take advantage of the polarity and hydrogen-bonding potential of the oxyanion hole region of the S1 specificity pocket. We demonstrate that placement of an anionic group within the oxyanion hole region of the catalytic site substantially enhances activity, with small flexible groups favored over bulkier ones. Ab initio pKa calculations suggest that the hydroxyl substituent frequently used for benzamidine moieties may be ionized to form an anionic group, consistent with the general trend. One nonamidine based substituent also shows promising activity.

About this Structure

1TX8 is a Single protein structure of sequence from Bos taurus with and as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

Design, synthesis, and evaluation of oxyanion-hole selective inhibitor substituents for the S1 subsite of factor Xa., Rumthao S, Lee O, Sheng Q, Fu W, Mulhearn DC, Crich D, Mesecar AD, Johnson ME, Bioorg Med Chem Lett. 2004 Oct 18;14(20):5165-70. PMID:15380220

Page seeded by OCA on Thu Feb 21 15:18:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tx8"
Personal tools