<p>PAN domains have significant functional versatility fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions [<cite idref="PUB00005679"/>]. These domains contain a hair-pin loop like structure, similar to knottins, but the pattern of disulphide bonds differs</p><p>It has been shown that, the N-terminal N domains of members of the plasminogen/hepatocyte growth factor family, the apple domains of the plasma prekallikrein/coagulation factor XI family, and domains of various nematode proteins belong to the same module superfamily, the PAN module [<cite idref="PUB00005679"/>]. PAN contains a conserved core of three disulphidebridges. In some members of the family there is an additionalfourth disulphide bridge that links the N and C termini of thedomain.</p> PAN-1 domain