1bqy
From Proteopedia
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'''PLASMINOGEN ACTIVATOR (TSV-PA) FROM SNAKE VENOM''' | '''PLASMINOGEN ACTIVATOR (TSV-PA) FROM SNAKE VENOM''' | ||
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[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Parry, M A.A.]] | [[Category: Parry, M A.A.]] | ||
| - | [[Category: | + | [[Category: Blood clotting]] |
| - | [[Category: | + | [[Category: Fibrinolysis]] |
| - | [[Category: | + | [[Category: Plasminogen activator]] |
| - | + | [[Category: Serine proteinase]] | |
| - | [[Category: | + | [[Category: Snake venom]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:50:58 2008'' |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:50, 2 May 2008
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 Page seeded by OCA on Fri May 2 11:50:58 2008
