STRUCTURE-FUNCTION-RELATIONSHIPS IN THE RECEPTOR FOR UROKINASE-TYPE PLASMINOGEN-ACTIVATOR - COMPARISON TO OTHER MEMBERS OF THE LY-6 FAMILY AND SNAKE-VENOM ALPHA-NEUROTOXINS

被引：236

作者：

PLOUG, M ^{[1
]}

ELLIS, V ^{[1
]}

机构：

[1] THROMBOSIS RES INST,LONDON SW3 6LR,ENGLAND

来源：

FEBS LETTERS | 1994年 / 349卷 / 02期

关键词：

UPA; UPAR; BUNGAROTOXIN; GLYCOSYL-PHOSPHATIDYLINOSITOL; CD59; MIRL;

D O I：

10.1016/0014-5793(94)00674-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 alpha-neurotoxins, suggesting that uPAR may adopt the same gross folding pattern as these structurally well characterized proteins. Structural aspects of the binding between a-neurotoxins and the acetylcholine receptor may have a major influence on future studies of the interaction between uPA and uPAR.

引用

页码：163 / 168

页数：6

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