The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins

FEBS Lett. 1999 Nov 12;461(1-2):63-7. doi: 10.1016/s0014-5793(99)01416-7.


Based on homology search and structure prediction methods we show that (1) the N-terminal N domains of members of the plasminogen/hepatocyte growth factor family, (2) the apple domains of the plasma prekallikrein/coagulation factor XI family, and (3) domains of various nematode proteins belong to the same module superfamily, hereafter referred to as the PAN module. The patterns of conserved residues correspond to secondary structural elements of the known three-dimensional structure of hepatocyte growth factor N domain, therefore we predict a similar fold for all members of this superfamily. Based on available functional informations on apple domains and N domains, it is clear that PAN modules have significant functional versatility, they fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans / chemistry
  • Databases, Factual
  • Factor XI / chemistry
  • Hepatocyte Growth Factor / chemistry*
  • Molecular Sequence Data
  • Plasminogen / chemistry*
  • Prekallikrein / chemistry*
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • Hepatocyte Growth Factor
  • Plasminogen
  • Factor XI
  • Prekallikrein