Annexins are a family of structurally related proteins with the common property of
peripheral binding to acidic phospholipid membranes. The canonical membrane binding mode
includes formation of a ternary complex between protein, calcium ions, and membrane.
Structurally, the annexin fold consists of a four-fold repeat of a ~70 aa sequence that
folds into a five-helix bundle
Specificity and diversity may be carried by the N-terminal domains, different for all
annexins, but may also be the consequence of interactions of annexins either with other
members of this protein family or other cellular partners. Indeed, the knowledge of the
three-dimensional structure of the conserved core of some annexins has not given sufficient
understanding of their biological function.
To address the issue of the complexity and diversity of the biological functions of this
protein family, the interactions of annexins with other proteins are investigated by a
combination of structural, cell and molecular biology methods:
- preparation of annexins and interacting proteins
- production of large quantities of these proteins
- X-ray crystallography
- low- and high-resolution electron microscopy
- fluorescence spectroscopy using synchrotron radiation
- search for cellular partners of annexins
- immunolocalisation of proteins within cells
- transfection experiments on the partners for annexins.