title: Three-dimensional structure of annexins.
abstract: Annexins constitute a family of structurally related calcium- and phospholipid-binding proteins whose molecular structure has been investigated in detail in the crystalline and membrane-bound form. Their polypeptide chain is folded into four or eight alpha-helical domains of similar structure with a central hydrophilic pore. Bound to phospholipid membranes, the four-domain arrangement of the annexin molecule is conserved. A peripheral binding mode has been well documented by electron microscopy and a variety of other techniques.
authors.affiliation: Abteilung für Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany. liemann@mol.biol.ethz.ch
authors.forename: S
authors.initials: S
authors.lastname: Liemann
authors.forename: R
authors.initials: R
authors.lastname: Huber
mesh_terms: D017302:Annexins / Q000648:ultrastructure*; D001665:Binding Sites; D002135:Calcium-Binding Proteins / Q000648:ultrastructure*; D006801:Humans; D007473:Ion Channels / Q000648:ultrastructure; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D017434:Protein Structure, Tertiary
chemical_list: D017302:Annexins; D002135:Calcium-Binding Proteins; D007473:Ion Channels; D008565:Membrane Proteins