This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2aiq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2aiq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aiq, resolution 1.54&Aring;" /> '''Crystal structure of...)
Line 1: Line 1:
-
[[Image:2aiq.gif|left|200px]]<br /><applet load="2aiq" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2aiq.gif|left|200px]]<br /><applet load="2aiq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2aiq, resolution 1.54&Aring;" />
caption="2aiq, resolution 1.54&Aring;" />
'''Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix'''<br />
'''Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix'''<br />
==Overview==
==Overview==
-
Protein C activation initiated by the thrombin-thrombomodulin complex, forms the major physiological anticoagulant pathway. Agkistrodon, contortrix contortrix protein C activator, a glycosylated single-chain, serine proteinase, activates protein C without relying on thrombomodulin., The crystal structures of native and inhibited Agkistrodon contortrix, contortrix protein C activator determined at 1.65 and 1.54 A resolutions, respectively, indicate the pivotal roles played by the positively charged, belt and the strategic positioning of the three carbohydrate moieties, surrounding the catalytic site in protein C recognition, binding, and, activation. Structural changes in the benzamidine-inhibited enzyme suggest, a probable function in allosteric regulation for the anion-binding site, located in the C-terminal extension, which is fully conserved in snake, venom serine proteinases, that preferentially binds Cl(1-) instead of, SO(4)(2-).
+
Protein C activation initiated by the thrombin-thrombomodulin complex forms the major physiological anticoagulant pathway. Agkistrodon contortrix contortrix protein C activator, a glycosylated single-chain serine proteinase, activates protein C without relying on thrombomodulin. The crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator determined at 1.65 and 1.54 A resolutions, respectively, indicate the pivotal roles played by the positively charged belt and the strategic positioning of the three carbohydrate moieties surrounding the catalytic site in protein C recognition, binding, and activation. Structural changes in the benzamidine-inhibited enzyme suggest a probable function in allosteric regulation for the anion-binding site located in the C-terminal extension, which is fully conserved in snake venom serine proteinases, that preferentially binds Cl(1-) instead of SO(4)(2-).
==About this Structure==
==About this Structure==
-
2AIQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agkistrodon_contortrix_contortrix Agkistrodon contortrix contortrix] with NAG, NDG, SO4, ACT, CL, BEN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Venombin_A Venombin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.74 3.4.21.74] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AIQ OCA].
+
2AIQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agkistrodon_contortrix_contortrix Agkistrodon contortrix contortrix] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=BEN:'>BEN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Venombin_A Venombin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.74 3.4.21.74] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIQ OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Venombin A]]
[[Category: Venombin A]]
-
[[Category: Arni, R.K.]]
+
[[Category: Arni, R K.]]
-
[[Category: Murakami, M.T.]]
+
[[Category: Murakami, M T.]]
[[Category: ACT]]
[[Category: ACT]]
[[Category: BEN]]
[[Category: BEN]]
Line 26: Line 26:
[[Category: snake venom serine proteinase]]
[[Category: snake venom serine proteinase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:09:01 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:49 2008''

Revision as of 14:27, 21 February 2008


2aiq, resolution 1.54Å

Drag the structure with the mouse to rotate

Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix

Overview

Protein C activation initiated by the thrombin-thrombomodulin complex forms the major physiological anticoagulant pathway. Agkistrodon contortrix contortrix protein C activator, a glycosylated single-chain serine proteinase, activates protein C without relying on thrombomodulin. The crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator determined at 1.65 and 1.54 A resolutions, respectively, indicate the pivotal roles played by the positively charged belt and the strategic positioning of the three carbohydrate moieties surrounding the catalytic site in protein C recognition, binding, and activation. Structural changes in the benzamidine-inhibited enzyme suggest a probable function in allosteric regulation for the anion-binding site located in the C-terminal extension, which is fully conserved in snake venom serine proteinases, that preferentially binds Cl(1-) instead of SO(4)(2-).

About this Structure

2AIQ is a Single protein structure of sequence from Agkistrodon contortrix contortrix with , , , , , and as ligands. Active as Venombin A, with EC number 3.4.21.74 Full crystallographic information is available from OCA.

Reference

Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator., Murakami MT, Arni RK, J Biol Chem. 2005 Nov 25;280(47):39309-15. Epub 2005 Sep 14. PMID:16162508

Page seeded by OCA on Thu Feb 21 16:27:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools