Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins

J Mol Biol. 1998 Feb 6;275(5):725-30. doi: 10.1006/jmbi.1997.1510.


Using a new method for construction and database searches of sequence consensus strings, we have identified a new superfamily of protein modules comprising laminin G, thrombospondin N and the pentraxin families. The conserved patterns correspond mainly to hydrophobic core residues located in central beta strands of the known three-dimensional structures of two pentraxins, the human C-reactive protein and the serum amyloid P-component. Thus, we predict a similar jellyroll fold for all members of this superfamily. In addition, the conservation of two exposed aspartate residues in the majority of superfamily members suggests hitherto unrecognised functional sites.

MeSH terms

  • Amino Acid Sequence
  • C-Reactive Protein / chemistry*
  • Humans
  • Laminin / chemistry*
  • Molecular Sequence Data
  • Protein Folding*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Serum Amyloid P-Component / chemistry*
  • Thrombospondins / chemistry*


  • Laminin
  • Serum Amyloid P-Component
  • Thrombospondins
  • PTX3 protein
  • C-Reactive Protein