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.

Abstract:

: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 alpha-neurotoxins and the acetylcholine receptor may have a major influence on future studies of the interaction between uPA and uPAR.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ploug M,Ellis V

doi

10.1016/0014-5793(94)00674-1

subject

Has Abstract

pub_date

1994-08-01 00:00:00

pages

163-8

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)00674-1

journal_volume

349

pub_type

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