2aip: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2aip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agkistrodon_contortrix_contortrix Agkistrodon contortrix contortrix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AIP FirstGlance]. <br> | <table><tr><td colspan='2'>[[2aip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agkistrodon_contortrix_contortrix Agkistrodon contortrix contortrix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AIP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aip OCA], [https://pdbe.org/2aip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aip RCSB], [https://www.ebi.ac.uk/pdbsum/2aip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aip ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aip OCA], [https://pdbe.org/2aip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aip RCSB], [https://www.ebi.ac.uk/pdbsum/2aip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aip ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VSPCA_AGKCO VSPCA_AGKCO] Snake venom serine protease that selectively cleaves the heavy chain of protein C (PROC). This activation is thrombomodulin-independent.<ref>PMID:3624272</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Agkistrodon contortrix contortrix]] | [[Category: Agkistrodon contortrix contortrix]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arni RK]] | |||
[[Category: Arni | [[Category: Murakami MT]] | ||
[[Category: Murakami | |||
Revision as of 10:24, 23 August 2023
Crystal structure of native protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrixCrystal structure of native protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix
Structural highlights
FunctionVSPCA_AGKCO Snake venom serine protease that selectively cleaves the heavy chain of protein C (PROC). This activation is thrombomodulin-independent.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein 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-). 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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