An active zymogen: unravelling the mystery of tissue-type plasminogen activator.

An active zymogen: unravelling the mystery of tissue-type plasminogen activator.
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活性酶原:揭开组织型纤溶酶原激活剂的神秘面纱。

DOI:
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发表时间:
1998
影响因子:
3.7
通讯作者:
W. Bode
W. Bode
中科院分区:
生物学2区
文献类型:
--
作者:
M. Stubbs;M. Renatus;W. Bode

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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.
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