In 1993, Huber and co-workers published the structure of an N-terminally truncated version
of human annexin A1 lacking the first 32 amino acid residues (PDB code: 1AIN). In 2001, we …

Annexins comprise a multigene family of Ca2+ and phospholipid-binding proteins. They
consist of a conserved C-terminal or core domain that confers Ca2+-dependent …

Annexin A11 is one of the 12 vertebrate subfamilies in the annexin superfamily of
calcium/phospholipid-binding proteins, distinguishable by long, non-homologous N-termini …

Annexin V was crystallized in the presence of a high concentration of calcium and the
structure refined at 1· 9 Å resolution. The crystals are triclinic (P1) with three molecules per …

Annexins constitute a family of phospholipid-and Ca2+-binding proteins involved in a variety
of membrane-related processes. The property of several annexins, including annexin A5, to …

The structure of recombinant human annexin III was solved to 1.8 Å resolution. Though
homologous to annexin I and V, the annexin III structure shows significant differences. The …

Two crystal forms (P6 3 and R3 of human annexin V have been crystallographically refined
at 2.3 Å and 2.0 Å resolution to R-values of 0.184 and 0.174, respectively, applying very tight …

Abstract cDNA coding for N‐terminally truncated human annexin I, a member of the family of
Ca2+‐dependent phospholipid binding proteins, has been cloned and expressed in …

Annexin V belongs to a family of eukaryotic calcium-dependent membrane-binding proteins.
The calcium-binding sites at the annexin− membrane interface have been investigated in …

The hallmark of the annexin super family of proteins is Ca2+-dependent binding to
phospholipid bilayers, a property that resides in the conserved core domain of these …