1bqy
From Proteopedia
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|PDB= 1bqy |SIZE=350|CAPTION= <scene name='initialview01'>1bqy</scene>, resolution 2.50Å | |PDB= 1bqy |SIZE=350|CAPTION= <scene name='initialview01'>1bqy</scene>, resolution 2.50Å | ||
|SITE= <scene name='pdbsite=A:Catalytic+Sites'>A</scene> and <scene name='pdbsite=B:Catalytic+Sites'>B</scene> | |SITE= <scene name='pdbsite=A:Catalytic+Sites'>A</scene> and <scene name='pdbsite=B:Catalytic+Sites'>B</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MAI:DEOXO-METHYLARGININE'>MAI</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqy OCA], [http://www.ebi.ac.uk/pdbsum/1bqy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bqy RCSB]</span> | ||
}} | }} | ||
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[[Category: snake venom]] | [[Category: snake venom]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:06:29 2008'' |
Revision as of 16:06, 30 March 2008
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| , resolution 2.50Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PLASMINOGEN ACTIVATOR (TSV-PA) FROM SNAKE VENOM
Overview
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.
About this Structure
1BQY is a Single protein structure of sequence from Viridovipera stejnegeri. Full crystallographic information is available from OCA.
Reference
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
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