1ddj
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CRYSTAL STRUCTURE OF HUMAN PLASMINOGEN CATALYTIC DOMAIN
OverviewOverview
Activation of the serine protease plasmin from its zymogen, plasminogen, is the key step in fibrinolysis leading to blood clot dissolution. It also, plays critical roles in cell migration, such as in tumor metastasis. Here, we report the crystal structure of an inactive S741A mutant of human, plasminogen catalytic domain at 2.0 A resolution. This structure permits a, direct comparison with that of the plasmin catalytic unit. Unique, conformational differences are present between these two structures that, are not seen in other zymogen-enzyme pairs of the trypsin family. The, functional significance of these differences and the structural basis of, plasminogen activation is discussed in the light of this new structure.
DiseaseDisease
Known diseases associated with this structure: Conjunctivitis, ligneous OMIM:[173350], Plasminogen Tochigi disease OMIM:[173350], Plasminogen deficiency, types I and II OMIM:[173350], Thrombophilia, dysplasminogenemic OMIM:[173350]
About this StructureAbout this Structure
1DDJ is a Single protein structure of sequence from Homo sapiens. Active as Plasmin, with EC number 3.4.21.7 Full crystallographic information is available from OCA.
ReferenceReference
Human plasminogen catalytic domain undergoes an unusual conformational change upon activation., Wang X, Terzyan S, Tang J, Loy JA, Lin X, Zhang XC, J Mol Biol. 2000 Jan 28;295(4):903-14. PMID:10656799
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