Ca(2+)- and Mg(2+)-dependent binding of annexin II and its complex to phospholipid vesicles; a comparative spectroscopic study.
The binding of annexin II (p36) and of its complex ((p36)2 (p11)2) to model phospholipid vesicles led to conformational changes of the proteins which were studied by fluorescence spectroscopy. Titrations with liposomes of different kinds showed that the presence of the p11 dimer in the complex enhances the conformational change of the annexin II. Comparative liposome titrations were carried out in the presence of Mg2+: the binding of the protein to liposome induced a much smaller protein conformational change in this case. Moreover, Ca2+ and phospholipid binding order experiments showed that the protein conformational change only occurred when both are bound.
Follenius-Wund
A
A
Laboratoire de Biophysique, URA CNRS 491, Université Louis Pasteur de Strasbourg, Faculté de Pharmacie, Illkirch, France.
Pigault
C
C
Gerard
D
D
D000818:Animals; D017306:Annexin A2 / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology*; D002417:Cattle; D008081:Liposomes / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology*; D010743:Phospholipids / Q000378:metabolism*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D017306:Annexin A2; D008081:Liposomes; D010743:Phospholipids; D008274:Magnesium; D002118:Calcium