Crystal structure of coagulogen, the clotting protein from horseshoe crab: A structural homologue of nerve growth factor

Andreas Bergner, Vaheh Oganessyan, Tatsushi Muta, Sadaaki Iwanaga, Dieter Typke, Robert Huber, Wolfram Bode

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

The clotting cascade system of the horseshoe crab (Limulus) is involved in both haemostasis and host defence. The cascade results in the conversion of coagulogen, a soluble protein, into an insoluble coagulin gel. The clotting enzyme excises the fragment peptide C from coagulogen, giving rise to aggregation of the monomers. The crystal structure of coagulogen reveals an elongated molecule that embraces the helical peptide C fragment. Cleavage and removal of the peptide C would expose an extended hydrophobic cove, which could interact with the hydrophobic edge of a second molecule, leading to a polymeric fibre. The C-terminal half of the coagulogen molecule exhibits a striking topological similarity to the neurotrophin nerve growth factor (NGF), providing the first evidence for a neurotrophin fold in invertebrates. Similarities between coagulogen and Spatzle, the Drosophila ligand of the receptor Toll, suggest that the neurotrophin fold might be considered more ancient and widespread than previously realized.

Original languageEnglish
Pages (from-to)6789-6797
Number of pages9
JournalEMBO Journal
Volume15
Issue number24
DOIs
Publication statusPublished - 1996 Jan 1

Keywords

  • Crystal structure
  • Cystine knot
  • Horseshoe crab
  • Nerve growth factor
  • Spatzle

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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