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A Cooperative Model for Receptor Recognition and Cell Adhesion: Evidence from the Molecular Packing in the 1.6-Å Crystal Structure of the Pheromone Er-1 from the Ciliated Protozoan Euplotes raikovi

The crystal structure of the pheromone Er-1 from the unicellular eukaryotic organism Euplotes raikovi was determined at 1.6 Å resolution and refined to a crystallographic R factor of 19.9%. In the tightly packed crystal, two extensive intermolecular helix-helix interactions arrange the Er-1 molecule...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1995-10, Vol.92 (22), p.10172-10176
Main Authors: Weiss, Manfred S., Anderson, Daniel H., Raffioni, Simona, Bradshaw, Ralph A., Ortenzi, Claudio, Luporini, Pierangelo, Eisenberg, David
Format: Article
Language:English
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Summary:The crystal structure of the pheromone Er-1 from the unicellular eukaryotic organism Euplotes raikovi was determined at 1.6 Å resolution and refined to a crystallographic R factor of 19.9%. In the tightly packed crystal, two extensive intermolecular helix-helix interactions arrange the Er-1 molecules into layers. Since the putative receptor of the pheromone is a membrane-bound protein, whose extracellular C-terminal domain is identical in amino acid sequence to the soluble pheromone, the interactions found in the crystal may mimic the pheromone-receptor interactions as they occur on a cell surface. Based on this, we propose a model for the interaction between soluble pheromone molecules and their receptors. In this model, strong pheromone-receptor binding emerges as a consequence of the cooperative utilization of several weak interactions. The model offers an explanation for the results of binding studies and may also explain the adhesion between cells that occurs during mating.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.92.22.10172