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

Citation
H. Tordai et al., 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 LETTER, 461(1-2), 1999, pp. 63-67
Citations number
29
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
461
Issue
1-2
Year of publication
1999
Pages
63 - 67
Database
ISI
SICI code
0014-5793(19991112)461:1-2<63:TPMTND>2.0.ZU;2-3
Abstract
Based on homology starch and structure prediction methods ne show that (1) the N-terminal N domains of members of the plasminogen/hepatocyte growth fa ctor family, (2) the apple domains of the plasma prekallikrein/coagulation factor XI family, and (3) domains of various nematode proteins belong to th e same module superfamily, hereafter referred to as the PAN module. The pat terns of conserved residues correspond to secondary structural elements of the known three-dimensional structure of hepatocyte growth factor: domain, therefore we predict a similar fold for all members of this superfamily. Ba sed on available functional informations on apple domains and N domains, it is clear that PAN modules have significant functional versatility, they fu lfill diverse biological functions by mediating protein-protein or protein- carbohydrate interactions. (C) 1999 Federation of European Biochemical Soci eties.