2aip: Difference between revisions

Revision as of 17:27, 21 February 2008

Crystal structure of native protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix

OverviewOverview

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 StructureAbout this Structure

2AIP 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.

ReferenceReference

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

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OCA

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-[[Image:2aip.gif|left|200px]]<br /><applet load="2aip" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2aip.gif|left|200px]]<br /><applet load="2aip" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2aip, resolution 1.65&Aring;" />
 '''Crystal structure of native protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix'''<br />
 ==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==
-AIP 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 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=2AIP OCA].
+AIP 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> 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=2AIP OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Venombin A]]
-[[Category: Arni, R.K.]]
+[[Category: Arni, R K.]]
-[[Category: Murakami, M.T.]]
+[[Category: Murakami, M T.]]
 [[Category: ACT]]
 [[Category: GOL]]
@@ Line 25: / Line 25: @@
 [[Category: trypsin-like enzyme]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:08:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:49 2008''