Structure—function relationships in the receptor for urokinase‐type plasminogen activator Comparison to other members of the Ly‐6 family and snake venom α‐neurotoxins

FEBS Letters

Ellis, Vincent¹  Ploug, Michael¹ 

[1] Finsen Laboratory, Rigshospitalet, Strandboulevarden 49, 2100 Copenhagen Ø, Denmark

关键词: uPA;    uPAR;    Bungarotoxin;    Glycosyl-phosphatidylinositol;    CD59;    MIRL;    uPA;    urokinase-type plasminogen activator;    uPAR;    urokinase-type plasminogen activator receptor PAI;    plasminogen activator inhibitor;   

DOI  :  10.1016/0014-5793(94)00674-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Plasminogen activation is regulated by the interaction between urokinase-type plasminogen activator (uPA) and its specific glycolipid-anchored cell surface receptor (uPAR). uPAR is composed of three homologous domains and is the only multi-domain member of the Ly-6 family of glycolipid-anchored membrane proteins. Recent evidence has highlighted similarities between the individual domains of uPAR and the large family of secreted, single domain snake venom α-neurotoxins, suggesting that uPAR may adopt the same gross folding pattern as these structurally well characterized proteins. Structural aspects of the binding between α-neurotoxins and the acetylcholine receptor may have a major influence on future studies of the interaction between uPA and uPAR.

【 授权许可】

Unknown