|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1bqy' size='340' side='right'caption='[[1bqy]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1bqy' size='340' side='right'caption='[[1bqy]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bqy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amnh_21054 Amnh 21054]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bqy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trimeresurus_stejnegeri Trimeresurus stejnegeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0GJ:L-ALPHA-GLUTAMYL-N-{(1S)-4-{[AMINO(IMINIO)METHYL]AMINO}-1-[(1S)-2-CHLORO-1-HYDROXYETHYL]BUTYL}GLYCINAMIDE'>0GJ</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0GJ:L-ALPHA-GLUTAMYL-N-{(1S)-4-{[AMINO(IMINIO)METHYL]AMINO}-1-[(1S)-2-CHLORO-1-HYDROXYETHYL]BUTYL}GLYCINAMIDE'>0GJ</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=1bqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqy OCA], [https://pdbe.org/1bqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bqy RCSB], [https://www.ebi.ac.uk/pdbsum/1bqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bqy 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=1bqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqy OCA], [https://pdbe.org/1bqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bqy RCSB], [https://www.ebi.ac.uk/pdbsum/1bqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bqy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/VSPPA_TRIST VSPPA_TRIST] Snake venom serine protease that activates plasminogen.<ref>PMID:7730329</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Amnh 21054]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bode, W]] | + | [[Category: Trimeresurus stejnegeri]] |
| - | [[Category: Parry, M A.A]] | + | [[Category: Bode W]] |
| - | [[Category: Blood clotting]] | + | [[Category: Parry MAA]] |
| - | [[Category: Fibrinolysis]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Plasminogen activator]]
| + | |
| - | [[Category: Serine proteinase]]
| + | |
| - | [[Category: Snake venom]]
| + | |
| Structural highlights
Function
VSPPA_TRIST Snake venom serine protease that activates plasminogen.[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
BACKGROUND: Trimeresurus stejnejeri venom plasminogen activator (TSV-PA) is a snake venom serine proteinase that specifically activates plasminogen. Snake venom serine proteinases form a subfamily of trypsin-like proteinases that are characterised by a high substrate specificity and resistance to inhibition. Many of these venom enzymes specifically interfere with haemostatic mechanisms and display a long circulating half-life. For these reasons several of them have commercial applications and are potentially attractive pharmacological tools. RESULTS: The crystal structure of TSV-PA has been determined to 2.5 A resolution and refined to an R factor of 17.8 (R free, 24.4). The enzyme, showing the overall polypeptide fold of trypsin-like serine proteinases, displays unique structural elements such as the presence of a phenylalanine at position 193, a C-terminal tail clamped via a disulphide bridge to the 99-loop, and a structurally conserved Asp97 residue. The presence of a cis proline at position 218 is in agreement with evolutionary relationships to glandular kallikrein. CONCLUSIONS: We postulate that Phe 193 accounts for the high substrate specificity of TSV-PA and renders it incapable of forming a stable complex with bovine pancreatic trypsin inhibitor and other extended substrates and inhibitors. Mutational studies previously showed that Asp97 is crucial for the plasminogenolytic activity of TSV-PA, here we identify the conservation of Asp97 in both types of mammalian plasminogen activator - tissue-type (tPA) and urokinase-type (uPA). It seems likely that Asp97 of tPA and uPA will have a similar role in plasminogen recognition. The C-terminal extension of TSV-PA is conserved among snake venom serine proteinases, although its function is unknown. The three-dimensional structure presented here is the first of a snake venom serine proteinase and provides an excellent template for modelling other homologous family members.
The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases.,Parry MA, Jacob U, Huber R, Wisner A, Bon C, Bode W Structure. 1998 Sep 15;6(9):1195-206. PMID:9753698[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang Y, Wisner A, Xiong Y, Bon C. A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning. J Biol Chem. 1995 Apr 28;270(17):10246-55. PMID:7730329 doi:10.1074/jbc.270.17.10246
- ↑ Parry MA, Jacob U, Huber R, Wisner A, Bon C, Bode W. The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases. Structure. 1998 Sep 15;6(9):1195-206. PMID:9753698
|
