1pml
From Proteopedia
Contents |
KRINGLE-KRINGLE INTERACTIONS IN MULTIMER KRINGLE STRUCTURES
Template:ABSTRACT PUBMED 8069221
Disease
[TPA_HUMAN] Note=Increased activity of TPA results in increased fibrinolysis of fibrin blood clots that is associated with excessive bleeding. Defective release of TPA results in hypofibrinolysis that can lead to thrombosis or embolism.
Function
[TPA_HUMAN] Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration.
About this Structure
1pml is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Padmanabhan K, Wu TP, Ravichandran KG, Tulinsky A. Kringle-kringle interactions in multimer kringle structures. Protein Sci. 1994 Jun;3(6):898-910. PMID:8069221