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. 1995 Jul 18;92(15):6793–6797. doi: 10.1073/pnas.92.15.6793

Considerations on the folding topology and evolutionary origin of cadherin domains.

L Shapiro 1, P D Kwong 1, A M Fannon 1, D R Colman 1, W A Hendrickson 1
PMCID: PMC41415  PMID: 7624321

Abstract

Cell-cell adhesion in zonula adherens and desmosomal junctions is mediated by cadherins, and recent crystal structures of the first domain from murine N-cadherin provide a plausible molecular basis for this adhesive action. A structure-based sequence analysis of this adhesive domain indicates that its fold is common to all extracellular cadherin domains. The cadherin folding topology is also shown to be similar to immunoglobulin-like domains and to other Greek-key beta-sandwich structures, as diverse as domains from plant cytochromes, bacterial cellulases, and eukaryotic transcription factors. Sequence similarities between cadherins and these other molecules are very low, however, and intron patterns are also different. On balance, independent origins for a favorable folding topology seem more likely than evolutionary divergence from an ancestor common to cadherins and immunoglobulins.

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