Premium
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
Author(s) -
Tordai Hedvig,
Bányai László,
Patthy László
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01416-7
Subject(s) - prekallikrein , protein superfamily , homology (biology) , biology , hepatocyte growth factor , superfamily , growth differentiation factor , domain (mathematical analysis) , protein structure , genetics , kringle domain , microbiology and biotechnology , biochemistry , amino acid , gene , receptor , kallikrein , mathematics , recombinant dna , bone morphogenetic protein , enzyme , mathematical analysis
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.