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| | <StructureSection load='2e3x' size='340' side='right'caption='[[2e3x]], [[Resolution|resolution]] 2.91Å' scene=''> | | <StructureSection load='2e3x' size='340' side='right'caption='[[2e3x]], [[Resolution|resolution]] 2.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E3X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E3X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GM6:3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-METHYLAMIDE'>GM6</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GM6:3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-METHYLAMIDE'>GM6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Russellysin Russellysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.58 3.4.24.58] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Russellysin Russellysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.58 3.4.24.58] </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=2e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e3x OCA], [http://pdbe.org/2e3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e3x RCSB], [http://www.ebi.ac.uk/pdbsum/2e3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2e3x 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=2e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e3x OCA], [https://pdbe.org/2e3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e3x RCSB], [https://www.ebi.ac.uk/pdbsum/2e3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e3x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VM3CX_DABSI VM3CX_DABSI]] Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.<ref>PMID:18616470</ref> [[http://www.uniprot.org/uniprot/SLLC1_DABSI SLLC1_DABSI]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref> [[http://www.uniprot.org/uniprot/SLLC2_DABSI SLLC2_DABSI]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref> | + | [[https://www.uniprot.org/uniprot/VM3CX_DABSI VM3CX_DABSI]] Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.<ref>PMID:18616470</ref> [[https://www.uniprot.org/uniprot/SLLC1_DABSI SLLC1_DABSI]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref> [[https://www.uniprot.org/uniprot/SLLC2_DABSI SLLC2_DABSI]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
2e3x is a 3 chain structure with sequence from Daboia russellii siamensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Activity: | Russellysin, with EC number 3.4.24.58 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[VM3CX_DABSI] Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.[1] [SLLC1_DABSI] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.[2] [SLLC2_DABSI] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.[3]
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
Russell's viper venom factor X activator (RVV-X) is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has been determined at 2.9 A resolution and shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle. A 6.5nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi-subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases.
Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases.,Takeda S, Igarashi T, Mori H FEBS Lett. 2007 Dec 22;581(30):5859-64. Epub 2007 Dec 3. PMID:18060879[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen HS, Chen JM, Lin CW, Khoo KH, Tsai IH. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 2008 Aug;275(15):3944-58. Epub 2008 Jul 4. PMID:18616470 doi:http://dx.doi.org/EJB6540
- ↑ Chen HS, Chen JM, Lin CW, Khoo KH, Tsai IH. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 2008 Aug;275(15):3944-58. Epub 2008 Jul 4. PMID:18616470 doi:http://dx.doi.org/EJB6540
- ↑ Chen HS, Chen JM, Lin CW, Khoo KH, Tsai IH. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 2008 Aug;275(15):3944-58. Epub 2008 Jul 4. PMID:18616470 doi:http://dx.doi.org/EJB6540
- ↑ Takeda S, Igarashi T, Mori H. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases. FEBS Lett. 2007 Dec 22;581(30):5859-64. Epub 2007 Dec 3. PMID:18060879 doi:10.1016/j.febslet.2007.11.062
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