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| <StructureSection load='3d65' size='340' side='right'caption='[[3d65]], [[Resolution|resolution]] 1.64Å' scene=''> | | <StructureSection load='3d65' size='340' side='right'caption='[[3d65]], [[Resolution|resolution]] 1.64Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3d65]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Eastern_brown_snake Eastern brown snake]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D65 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3D65 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3d65]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Pseudonaja_textilis_textilis Pseudonaja textilis textilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D65 FirstGlance]. <br> |
- | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3byb|3byb]]</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></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </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=3d65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d65 OCA], [https://pdbe.org/3d65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d65 RCSB], [https://www.ebi.ac.uk/pdbsum/3d65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d65 ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3d65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d65 OCA], [http://pdbe.org/3d65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d65 RCSB], [http://www.ebi.ac.uk/pdbsum/3d65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d65 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/VKT1_PSETT VKT1_PSETT]] Strongly inhibits plasmin (Ki=0.44 nM) and trypsin (Ki=0.42 nM). Has little effect on plasma (Ki=1870 nM) and tissue (Ki=12900 nM) kallikreins. In vivo, reduces bleeding in a small animal model.<ref>PMID:10847427</ref> <ref>PMID:12406072</ref> <ref>PMID:16707925</ref> <ref>PMID:19236611</ref> <ref>PMID:21843588</ref> <ref>PMID:23335990</ref> | + | [https://www.uniprot.org/uniprot/VKT1_PSETT VKT1_PSETT] Strongly inhibits plasmin (Ki=0.44 nM) and trypsin (Ki=0.42 nM). Has little effect on plasma (Ki=1870 nM) and tissue (Ki=12900 nM) kallikreins. In vivo, reduces bleeding in a small animal model.<ref>PMID:10847427</ref> <ref>PMID:12406072</ref> <ref>PMID:16707925</ref> <ref>PMID:19236611</ref> <ref>PMID:21843588</ref> <ref>PMID:23335990</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| <jmolCheckbox> | | <jmolCheckbox> |
| <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d6/3d65_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d6/3d65_consurf.spt"</scriptWhenChecked> |
- | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| </jmolCheckbox> | | </jmolCheckbox> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
- | [[Category: Eastern brown snake]]
| + | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Trypsin]] | + | [[Category: Pseudonaja textilis textilis]] |
- | [[Category: Guddat, L W]] | + | [[Category: Guddat LW]] |
- | [[Category: Jersey, J de]]
| + | [[Category: Lavin MF]] |
- | [[Category: Lavin, M F]] | + | [[Category: Masci PP]] |
- | [[Category: Masci, P P]] | + | [[Category: Millers E-KI]] |
- | [[Category: Millers, E K.I]] | + | [[Category: De Jersey J]] |
- | [[Category: Blood]]
| + | |
- | [[Category: Calcium]]
| + | |
- | [[Category: Coagulation]]
| + | |
- | [[Category: Digestion]]
| + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Hydrolase inhibitor-hydrolase complex]]
| + | |
- | [[Category: Metal-binding]] | + | |
- | [[Category: Protease]]
| + | |
- | [[Category: Secreted]]
| + | |
- | [[Category: Serine protease]]
| + | |
- | [[Category: Serine protease inhibitor]]
| + | |
- | [[Category: Zymogen]]
| + | |
| Structural highlights
Function
VKT1_PSETT Strongly inhibits plasmin (Ki=0.44 nM) and trypsin (Ki=0.42 nM). Has little effect on plasma (Ki=1870 nM) and tissue (Ki=12900 nM) kallikreins. In vivo, reduces bleeding in a small animal model.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Masci PP, Whitaker AN, Sparrow LG, de Jersey J, Winzor DJ, Watters DJ, Lavin MF, Gaffney PJ. Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model. Blood Coagul Fibrinolysis. 2000 Jun;11(4):385-93. PMID:10847427
- ↑ Filippovich I, Sorokina N, Masci PP, de Jersey J, Whitaker AN, Winzor DJ, Gaffney PJ, Lavin MF. A family of textilinin genes, two of which encode proteins with antihaemorrhagic properties. Br J Haematol. 2002 Nov;119(2):376-84. PMID:12406072
- ↑ Flight S, Johnson L, Trabi M, Gaffney P, Lavin M, de Jersey J, Masci P. Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents. Pathophysiol Haemost Thromb. 2005;34(4-5):188-93. PMID:16707925 doi:http://dx.doi.org/10.1159/000092421
- ↑ Flight SM, Johnson LA, Du QS, Warner RL, Trabi M, Gaffney PJ, Lavin MF, de Jersey J, Masci PP. Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss. Br J Haematol. 2009 Apr;145(2):207-11. doi: 10.1111/j.1365-2141.2009.07605.x., Epub 2009 Feb 22. PMID:19236611 doi:http://dx.doi.org/10.1111/j.1365-2141.2009.07605.x
- ↑ Earl ST, Richards R, Johnson LA, Flight S, Anderson S, Liao A, de Jersey J, Masci PP, Lavin MF. Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms. Biochimie. 2012 Feb;94(2):365-73. doi: 10.1016/j.biochi.2011.08.003. Epub 2011, Aug 11. PMID:21843588 doi:http://dx.doi.org/10.1016/j.biochi.2011.08.003
- ↑ Millers EK, Johnson LA, Birrell GW, Masci PP, Lavin MF, de Jersey J, Guddat LW. The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake. PLoS One. 2013;8(1):e54104. doi: 10.1371/journal.pone.0054104. Epub 2013 Jan 15. PMID:23335990 doi:10.1371/journal.pone.0054104
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