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| | <StructureSection load='2aip' size='340' side='right'caption='[[2aip]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='2aip' size='340' side='right'caption='[[2aip]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2aip]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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"><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=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Venombin_A Venombin A], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.74 3.4.21.74] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aip OCA], [http://pdbe.org/2aip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aip RCSB], [http://www.ebi.ac.uk/pdbsum/2aip PDBsum], [http://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 == |
| - | [[http://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> | + | [[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]] |
| Structural highlights
Function
[VSPCA_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 PubMed
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-).
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
- ↑ Kisiel W, Kondo S, Smith KJ, McMullen BA, Smith LF. Characterization of a protein C activator from Agkistrodon contortrix contortrix venom. J Biol Chem. 1987 Sep 15;262(26):12607-13. PMID:3624272
- ↑ Murakami MT, Arni RK. 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. J Biol Chem. 2005 Nov 25;280(47):39309-15. Epub 2005 Sep 14. PMID:16162508 doi:10.1074/jbc.M508502200
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