Journal article

Membrane-induced folding and structure of membrane-bound annexin A1 N-terminal peptides: Implications for annexin-induced membrane aggregation

Nien-Jen Hu, Jeremy Bradshaw, Hans Lauter, Julia Buckingham, Egle Solito, Andreas Hofmann

Biophysical Journal | CELL PRESS | Published : 2008

Abstract

Annexins constitute a family of calcium-dependent membrane-binding proteins and can be classified into two groups, depending on the length of the N-terminal domain unique for each individual annexin. The N-terminal domain of annexin A1 can adopt an alpha-helical conformation and has been implicated in mediating the membrane aggregation behavior of this protein. Although the calcium-independent interaction of the annexin A1 N-terminal domain has been known for some time, there was no structural information about the membrane interaction of this secondary membrane-binding site of annexin A1. This study used circular dichroism spectroscopy to show that a rat annexin A1 N-terminal peptide posses..

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University of Melbourne Researchers