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The crystal structure of the catalytic domain of human urokinase-type plasminogen activator.

Abstract:

BACKGROUND: Urokinase-type plasminogen activator (u-PA) promotes fibrinolysis by catalyzing the conversion of plasminogen to the active protease plasmin via the cleavage of a peptide bond. When localized to the external cell surface it contributes to tissue remodelling and cellular migration; inhibition of its activity impedes the spread of cancer. u-PA has three domains: an N-terminal receptor-binding growth factor domain, a central kringle domain and a C-terminal catalytic protease domain. ...

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Publication status:
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Authors


Spraggon, G More by this author
Phillips, C More by this author
Ponting, CP More by this author
Saunders, D More by this author
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Journal:
Structure (London, England : 1993)
Volume:
3
Issue:
7
Pages:
681-691
Publication date:
1995-07-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:ad4baf0e-3f13-4218-9477-b2d0a9b0e6b4
Source identifiers:
14498
Local pid:
pubs:14498

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