Getting knotted: a model for the structure and activation of Spätzle

Trends Biochem Sci. 1998 Jul;23(7):239-42. doi: 10.1016/s0968-0004(98)01216-x.


Sequence analyses show that Spätzle, the Drosophila melanogaster Toll-receptor ligand, shows striking similarity to nerve growth factor and coagulogen. Comparative modelling suggests that Spätzle adopts a cystine-knot fold and forms a dimer that contains a single, intermolecular disulphide bridge. Proteolytically cleaved Spätzle could therefore dimerize and activate the Toll receptor by inducing receptor dimerization.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blood Proteins / genetics
  • Drosophila Proteins*
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism
  • Insect Proteins / chemistry*
  • Insect Proteins / genetics
  • Insect Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Nerve Growth Factors / genetics
  • Protein Conformation
  • Sequence Homology, Amino Acid


  • Blood Proteins
  • Drosophila Proteins
  • Insect Proteins
  • Nerve Growth Factors
  • coagulogen
  • spz protein, Drosophila