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

. 1998 Feb 6;275(5):725-30.

doi: 10.1006/jmbi.1997.1510.

Affiliations

• PMID: 9480764
• DOI: 10.1006/jmbi.1997.1510

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

G Beckmann et al. J Mol Biol. 1998.

Abstract

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.

Copyright 1998 Academic Press Limited

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