The annexins comprise a family of soluble Ca2+-and phospholipid-binding proteins.
Although highly similar in three-dimensional structure, different annexins are likely to exhibit …

Conformational stability of the membrane-binding protein annexin V E17G has been
determined by high-sensitivity differential scanning microcalorimetry (DSC) measurements …

Revised Manuscript Received August 24, 1994® abstract: Annexins V and VI are two
members of the annexin protein family, each of which associate with phospholipid vesicles …

The annexin fold consists of four 70-residue domains with markedly homologous sequences
and nearly identical structures. Each domain contains five helices designated A to E …

The calcium binding properties of annexin I as observed by thermodynamic DSC studies
have been compared to the structural information obtained from X-ray investigation. The …

Limited proteolysis of the core domain of the 36‐kDa protein p36 by trypsin gives a first
insight into the structural organization of the four annexin repeats. Trypsin opens only a …

Crystallographic studies have shown that the binding of calcium to domain III of annexin V is
accompanied by a large conformational change involving surface exposure of Trp187. Here …

Proteins of the annexin family constitute very attractive models because of their four∼ 70
residue domains, D1 to D4, exhibiting an identical topology comprising five helix segments …

Recent studies have revealed that binding of annexin I to phospholipids induces the
formation of a second phospholipid binding site. It is shown that the N terminus on the …

All the functions of annexins in vitro as well as in vivo are mediated and probably regulated
by calcium. We have used recombinant annexin I, synthesized by Escherichia coli, and we …