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| | <StructureSection load='2f3c' size='340' side='right'caption='[[2f3c]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2f3c' size='340' side='right'caption='[[2f3c]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f3c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Assassin_bug Assassin bug] and [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F3C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2f3c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Triatoma_infestans Triatoma infestans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F3C 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></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=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=2f3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f3c OCA], [https://pdbe.org/2f3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f3c RCSB], [https://www.ebi.ac.uk/pdbsum/2f3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f3c 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=2f3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f3c OCA], [https://pdbe.org/2f3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f3c RCSB], [https://www.ebi.ac.uk/pdbsum/2f3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f3c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Assassin bug]] | + | [[Category: Bos taurus]] |
| - | [[Category: Bovin]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trypsin]] | + | [[Category: Triatoma infestans]] |
| - | [[Category: Barbosa, J A.R G]] | + | [[Category: Barbosa JARG]] |
| - | [[Category: Campos, I T.N]] | + | [[Category: Campos ITN]] |
| - | [[Category: Tanaka, A S]] | + | [[Category: Tanaka AS]] |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Kazal-type domain]]
| + | |
| - | [[Category: Serine protease - inhibitor complex]]
| + | |
| Structural highlights
Function
TRY1_BOVIN
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
Blood coagulation is an important process in haemostasis, and disorders of blood coagulation can lead to an increased risk of haemorrhage and thrombosis. Coagulation is highly conserved in mammals and has been comprehensively studied in humans in the investigation of bleeding or thrombotic diseases. Some substances can act as inhibitors of blood coagulation and may affect one or multiple enzymes throughout the process. A specific thrombin inhibitor called infestin has been isolated from the midgut of the haematophagous insect Triatoma infestans. Infestin is a member of the nonclassical Kazal-type serine protease inhibitors and is composed of four domains, all of which have a short central alpha-helix and a small antiparallel beta-sheet. Domains 1 and 4 of infestin (infestins 1 and 4) possess specific inhibitory activities. Infestin 1 inhibits thrombin, while infestin 4 is an inhibitor of factor XIIa, plasmin and factor Xa. Here, the structure determination and structural analysis of infestin 1 complexed with trypsin and of infestin 4 alone are reported. Through molecular modelling and docking, it is suggested that the protein-protein binding site is conserved in the infestin 1-thrombin complex compared with other Kazal-type inhibitors. Infestin 4 is able to bind factor XIIa, and the F9N and N11R mutants selected by phage display were shown to be more selective for factor XIIa in comparison to the wild type.
The Kazal-type inhibitors infestins 1 and 4 differ in specificity but are similar in three-dimensional structure.,Campos IT, Souza TA, Torquato RJ, De Marco R, Tanaka-Azevedo AM, Tanaka AS, Barbosa JA Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):695-702. Epub 2012 May 17. PMID:22683792[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Campos IT, Souza TA, Torquato RJ, De Marco R, Tanaka-Azevedo AM, Tanaka AS, Barbosa JA. The Kazal-type inhibitors infestins 1 and 4 differ in specificity but are similar in three-dimensional structure. Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):695-702. Epub 2012 May 17. PMID:22683792 doi:10.1107/S0907444912009067
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