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PDBsum entry 4dur
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References listed in PDB file
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Key reference
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Title
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The X-Ray crystal structure of full-Length human plasminogen.
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Authors
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R.H.Law,
T.Caradoc-Davies,
N.Cowieson,
A.J.Horvath,
A.J.Quek,
J.A.Encarnacao,
D.Steer,
A.Cowan,
Q.Zhang,
B.G.Lu,
R.N.Pike,
A.I.Smith,
P.B.Coughlin,
J.C.Whisstock.
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Ref.
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Cell Rep, 2012,
1,
185-190.
[DOI no: ]
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PubMed id
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Abstract
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Plasminogen is the proenzyme precursor of the primary fibrinolytic protease
plasmin. Circulating plasminogen, which comprises a Pan-apple (PAp) domain, five
kringle domains (KR1-5), and a serine protease (SP) domain, adopts a closed,
activation-resistant conformation. The kringle domains mediate interactions with
fibrin clots and cell-surface receptors. These interactions trigger plasminogen
to adopt an open form that can be cleaved and converted to plasmin by
tissue-type and urokinase-type plasminogen activators. Here, the structure of
closed plasminogen reveals that the PAp and SP domains, together with chloride
ions, maintain the closed conformation through interactions with the kringle
array. Differences in glycosylation alter the position of KR3, although in all
structures the loop cleaved by plasminogen activators is inaccessible. The
ligand-binding site of KR1 is exposed and likely governs proenzyme recruitment
to targets. Furthermore, analysis of our structure suggests that KR5 peeling
away from the PAp domain may initiate plasminogen conformational change.
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