Abstract:
:In contrast to almost all other proteinases, human tissue-type plasminogen activator (tPA) is also proteolytically active in its zymogen or single-chain form. The closely related plasminogen activator isolated from vampire bat saliva (vPA) acts exclusively in the single-chain form, lacking the requisite cleavage site for proteolytic activation. Recent structural studies on the proteolytic domains of vPA and human tPA in two- and single-chain forms reveal the mechanism of this anomalous activity. The PA-catalyzed proteolytic conversion of plasminogen to plasmin, responsible for the initiation of fibrinolysis, is fibrin-dependent; comparative structural analysis of the plasminogen activators provides clues as to the role of fibrin as cofactor.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Stubbs MT,Renatus M,Bode Wdoi
10.1515/bchm.1998.379.2.95subject
Has Abstractpub_date
1998-02-01 00:00:00pages
95-103issue
2eissn
1431-6730issn
1437-4315journal_volume
379pub_type
杂志文章,评审abstract::Seven purified proteins may be combined to reconstitute regulated, promoter-dependent RNA polymerase II transcription: five general transcription factors, Mediator, and RNA polymerase II. The entire system has been conserved across species from yeast to humans. The structure of RNA polymerase II, consisting of 10 poly...
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journal_title:Biological chemistry
pub_type: 杂志文章,评审
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更新日期:2020-05-26 00:00:00
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更新日期:2005-05-01 00:00:00
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更新日期:2010-11-01 00:00:00
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pub_type: 杂志文章,评审
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pub_type: 评论,杂志文章
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pub_type: 杂志文章
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更新日期:2002-09-01 00:00:00
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pub_type: 杂志文章
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更新日期:2007-04-01 00:00:00