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Structure comparison of the pheromones Er-1, Er-10, and Er-2 from Euplotes raikovi

✍ Scribed by Peter Luginbühl; Marcel Ottiger; Siggi Mronga; Kurt WÜthrich

Publisher
Cold Spring Harbor Laboratory Press
Year
1994
Tongue
English
Weight
896 KB
Volume
3
Category
Article
ISSN
0961-8368

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✦ Synopsis

Abstract

The NMR structures of the homologous pheromones E__r__‐1, E__r__‐10, and E__r__‐2 from the ciliated protozoan Euplotes raikovi are compared. For all 3 proteins the molecular architecture is made up of an antiparallel 3‐helix bundle. The preservation of the core part of the structure is directly manifested by similar patterns of slowed backbone amide proton exchange rates, hydrogen bond formation, and relative solvent accessibility. To align the 6 half‐cystine residues in the individual sequences within the preserved 3‐dimensional core structure, several deletions and insertions had to be introduced that differ from those previously proposed on the basis of the primary structures. Of special interest is a deletion in the second helix of E__r__‐2, which is accommodated by a transition from an α‐helix in E__r__‐1 and E__r__‐10 to a 3~10~‐helix in E__r__‐2. The most significant structural differences are located in the C‐terminal part of the proteins, which may have an important role in specific receptor recognition.

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