Cellular and Molecular Life Sciences CMLS

, Volume 53, Issue 6, pp 516–521

Three-dimensional structure of annexins

  • S. Liemann
  • R. Huber

DOI: 10.1007/s000180050065

Cite this article as:
Liemann, S. & Huber, R. CMLS, Cell. mol. life sci. (1997) 53: 516. doi:10.1007/s000180050065

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 α-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.

Key words. Annexin; crystal structure; electron microscopy; interfacial membrane proteins; ion channel.

Copyright information

© Birkhäuser Verlag Basel, 1997

Authors and Affiliations

  • S. Liemann
    • 1
  • R. Huber
    • 1
  1. 1.Abteilung für Strukturforschung, Max-Planck-Institut für Biochemie, D-82152 Martinsried (Germany)DE