Three-Finger Proteins from the Ly6/uPAR Family: Functional Diversity within One Structural Motif

Biochemistry (Mosc). 2017 Dec;82(13):1702-1715. doi: 10.1134/S0006297917130090.


The discovery in higher animals of proteins from the Ly6/uPAR family, which have structural homology with snake "three-finger" neurotoxins, has generated great interest in these molecules and their role in the functioning of the organism. These proteins have been found in the nervous, immune, endocrine, and reproductive systems of mammals. There are two types of the Ly6/uPAR proteins: those associated with the cell membrane by GPI-anchor and secreted ones. For some of them (Lynx1, SLURP-1, SLURP-2, Lypd6), as well as for snake α-neurotoxins, the target of action is nicotinic acetylcholine receptors, which are widely represented in the central and peripheral nervous systems, and in many other tissues, including epithelial cells and the immune system. However, the targets of most proteins from the Ly6/uPAR family and the mechanism of their action remain unknown. This review presents data on the structural and functional properties of the Ly6/uPAR proteins, which reveal a variety of functions within a single structural motif.

Publication types

  • Review

MeSH terms

  • Animals
  • Antigens, Ly / chemistry*
  • Glycosylphosphatidylinositols
  • Humans
  • Neurotoxins / chemistry
  • Receptors, Urokinase Plasminogen Activator / chemistry*
  • Receptors, Urokinase Plasminogen Activator / physiology
  • Structure-Activity Relationship


  • Antigens, Ly
  • Glycosylphosphatidylinositols
  • Neurotoxins
  • Receptors, Urokinase Plasminogen Activator