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
Research output: Contribution to journal › Review › Research › peer-review
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.
Original language | English |
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Journal | FEBS Letters |
Volume | 349 |
Issue number | 2 |
Pages (from-to) | 163-8 |
Number of pages | 6 |
ISSN | 0014-5793 |
Publication status | Published - 1 Aug 1994 |
Externally published | Yes |
- Amino Acid Sequence, Animals, Antigens, Ly, Molecular Sequence Data, Neurotoxins, Structure-Activity Relationship, Urokinase-Type Plasminogen Activator, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Review
Research areas
ID: 178216007