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Visualization of Annexin I Binding to Calcium‐Induced Phosphatidylserine Domains
Author(s) -
Janshoff Andreas,
Ross Michaela,
Gerke Volker,
Steinem Claudia
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010803)2:7/8<587::aid-cbic587>3.0.co;2-q
Subject(s) - phosphatidylserine , annexin , chemistry , biophysics , phospholipid , annexin a2 , crystallography , lipid bilayer , biochemistry , membrane , biology , cell
A monomolecular protein adsorption was observed for the binding of annexin I to phosphatidylserine‐enriched lipid domains. The interactions of this membrane‐associated protein (red in the picture; green=N terminus, •=Ca 2+ ‐binding site) with phospholipid bilayers immobilized on mica were visualized by scanning force microscopy. Domain formation in 1,2‐dipalmitoyl‐ sn ‐glycero‐3‐phosphocholine/‐phosphoserine layers was induced by Ca 2+ ions rather than by the protein itself, as demonstrated by time‐of‐flight secondary‐ion mass spectrometric analysis and lateral force microscopy.