Epitope mapping of annexin I: antibodies that compete with phospholipids and calcium recognize amino acids 42-99.
To understand further the structural basis of phospholipid binding by annexin I, three monoclonal antibodies that compete with Ca2+ and phospholipids for binding of annexin I were used to screen an expression library containing fragments of bovine annexin I cDNA. In all, 15 clones were isolated, and all contain overlapping fragments of the cDNA. The smallest unit common to all of the clones encodes amino acids 42-99 of annexin I, representing a portion of the first repeat domain. This demonstrates that recognition of a single domain of annexin I is sufficient to completely block phospholipid binding, and implies that the first repeat may contribute to phospholipid binding by annexin I.
Ernst
J D
JD
Department of Medicine, University of California, San Francisco.
D000595:Amino Acid Sequence; D000818:Animals; D017305:Annexin A1 / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D000911:Antibodies, Monoclonal / Q000494:pharmacology; D001665:Binding Sites; D001666:Binding Sites, Antibody; D002118:Calcium / Q000378:metabolism*; D002417:Cattle; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D000939:Epitopes / Q000032:analysis*; D015723:Gene Library; D006801:Humans; D008969:Molecular Sequence Data; D010743:Phospholipids / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D017305:Annexin A1; D000911:Antibodies, Monoclonal; D000939:Epitopes; D010743:Phospholipids; D004247:DNA; D002118:Calcium