New insights into the structure and function of the plasminogen/plasmin system
RHP Law, D Abu-Ssaydeh, JC Whisstock - Current opinion in structural …, 2013 - Elsevier
RHP Law, D Abu-Ssaydeh, JC Whisstock
Current opinion in structural biology, 2013•ElsevierHighlights•Plasminogen initially binds C-terminal lysine containing receptors through kringle
1.•Plasminogen conformational change is triggered through lysine binding to kringle
5.•Glycosylation patterns change plasminogen shape, stability and biological
function.•Bacterial virulence factors evade the mechanism that regulates plasminogen
activation.Plasminogen is the zymogen form of plasmin, an enzyme that plays a fundamental
role in the dissolution of fibrin clots, the extracellular matrix and other key proteins involved …
1.•Plasminogen conformational change is triggered through lysine binding to kringle
5.•Glycosylation patterns change plasminogen shape, stability and biological
function.•Bacterial virulence factors evade the mechanism that regulates plasminogen
activation.Plasminogen is the zymogen form of plasmin, an enzyme that plays a fundamental
role in the dissolution of fibrin clots, the extracellular matrix and other key proteins involved …
Highlights
- Plasminogen initially binds C-terminal lysine containing receptors through kringle 1.
- Plasminogen conformational change is triggered through lysine binding to kringle 5.
- Glycosylation patterns change plasminogen shape, stability and biological function.
- Bacterial virulence factors evade the mechanism that regulates plasminogen activation.
Plasminogen is the zymogen form of plasmin, an enzyme that plays a fundamental role in the dissolution of fibrin clots, the extracellular matrix and other key proteins involved in immunity and tissue repair. Comprising seven distinct domains (an N-terminal Pan-apple domain (PAp), 5 kringle domains (KR) and the serine protease domain (SP)), plasminogen undergoes a complex, incompletely understood conformational change that is key to its activation. Here, we review our current understanding of the structural basis for plasminogen activation with regard to new insights derived from crystallographic and biochemical studies.
Elsevier